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(2S,4S)-4-fluoroproline + 2-oxoglutarate + O2
(2S)-4-oxoproline + fluoride
-
development and evaluation of an assay method that continuously and directly detects turnover of the proline-containing substrate. The assay is based on (2S,4S)-4-fluoroproline, a proline analogue that is transformed into (2S)-4-oxoproline and inorganic fluoride by P4H using a fluoride ion-selective electrode for detection
-
-
?
(Ala-Pro-Gly)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
recombinant enzyme
-
?
(Ala-Thr-Pro-Pro-Pro-Val)3 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
?
(ATPPPV)3 + 2-oxoglutarate + O2
trans-4-hydroxy-L-proline (ATPPPV)3 + succinate + CO2
-
-
-
-
?
(Gly-Ala-Pro)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
(Gly-Pro-4Hyp)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
?
(Gly-Pro-Ala)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
(Gly-Pro-Pro)10 + 2-oxoglutarate + O2
?
(GPP)10 + 2-oxoglutarate + O2
?
-
-
-
-
?
(L-Pro-L-Ala-L-Pro-L-Lys)2 + 2-oxoglutarate + O2
(L-Pro-L-Ala-L-Pro-L-Lys)2-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Ala-L-Pro-L-Lys)3 + 2-oxoglutarate + O2
(L-Pro-L-Ala-L-Pro-L-Lys)3-trans-4-hydroxy-L-proline + succinate + CO2
(L-Pro-L-Glu-L-Pro-L-Pro-L-Ala)5 L-proline + 2-oxoglutarate + O2
(L-Pro-L-Glu-L-Pro-L-Pro-L-Ala)5 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
(L-Pro-L-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
44.8% of the activity with (L-Pro-L-Glu-L-Pro-L-Pro-L-Ala)5 L-proline
-
-
?
(L-Pro-L-Pro-Gly)2 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)2-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
(L-prolylglycyl-L-prolyl)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
-
molecular weight of the peptide substrate: about 4000
-
?
(L-Ser-L-Pro)19 L-proline + 2-oxoglutarate + O2
(L-Ser-L-Pro)19 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(L-Ser-L-Pro-L-Ala-L-Pro-L-Pro)5 L-proline + 2-oxoglutarate + O2
(L-Ser-L-Pro-L-Ala-L-Pro-L-Pro)5 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(L-Ser-L-Pro-L-Glu-L-Pro-L-Pro)5 L-proline + 2-oxoglutarate + O2
(L-Ser-L-Pro-L-Glu-L-Pro-L-Pro)5 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(L-Ser-L-Pro-L-Lys-L-Pro-L-Pro)5 L-proline + 2-oxoglutarate + O2
(L-Ser-L-Pro-L-Lys-L-Pro-L-Pro)5 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Ala-Gly)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
?
(Pro-Ala-Pro-Lys)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
(Pro-Glu-Pro-Pro-Ala)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
(Pro-Gly-Pro)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
(Pro-Pro-Gly)10 + 2-oxoglutarate + O2
? + succinate + CO2
(Pro-Pro-Gly)10 + 2-oxoglutarate + O2
trans-4-hydroxy-L-proline (Pro-Pro-Gly)10 + succinate + CO2
-
-
-
?
(Pro-Pro-Gly)10 + O2
?
-
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
(Pro-Pro-Gly)2 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)2 trans-4-hydroxy-L-proline + succinate + CO2
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
(Ser-Pro)5 + O2
?
-
the (Ser-Pro)5 peptide is found only in molecules A and C of the four polypeptides forming the enzyme
-
-
?
(Ser-Pro-Lys-Pro-Pro)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
100-amino acid alpha1(I) collagen fragment + 2-oxoglutarate + O2
?
-
-
-
-
r
100-amino acid alpha1(I) collagen fragment L-proline + 2-oxoglutarate + O2
100-amino acid alpha1(I) collagen fragment trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
510-amino acid alpha1(I) collagen fragment + 2-oxoglutarate + O2
?
-
-
-
-
r
510-amino acid alpha1(I) collagen fragment L-proline + 2-oxoglutarate + O2
510-amino acid alpha1(I) collagen fragment trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
Arg-Gly-(Pro-Pro-Gly)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
Argonaute 2 + 2-oxoglutarate + O2
4-hydroxyproline-Argonaute 2 + succinate + CO2
-
regulation of Ago 2 protein activity via substrate protein stability involving Ago Pro700 residue, the Ago protein mutant P700A is destabilized, overview
-
-
?
Argonaute protein + 2-oxoglutarate + O2
4-hydroxyproline-Argonaute protein + succinate + CO2
-
i.e. GERp95 or Golgi endoplasmic reticulum protein 95 kDa. Recombinant substrate proteins expressed in HeLa S3 cells. Ago2 is a cytoplasmically exposed, peripheral membrane protein that exists in a protease-resistant complex. Hydroxylation of Pro700, which is important for Ago2 stability, but not of Ago1 or Ago3 stability, identification by mass spectrometric analysis. In vitro, both Ago2 and Ago4 seem to be more efficiently hydroxylated than Ago1 and Ago3 by recombinant human isozyme C-P4H(I)
-
-
?
Asp-Ala-Leu-Thr-Leu-Leu-Ala-Pro-Ala-Ala-Gly-Asp-Thr-Ile-Ile-Ser-Leu-Phe-Gly + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
peptide representing hypoxia-inducible transcription factor alpha sequences
-
?
Asp-Leu-Asp-Leu-Glu-Met-Leu-Ala-Pro-Tyr-Ile-Pro-Met-Asp-Asp-Asp-Phe-Gln-Leu + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
peptide representing hypoxia-inducible transcription factor alpha sequences
-
?
biotin-Ahx-DLDLEALAP564YIPADDDFQL + 2-oxoglutarate + O2
?
-
19mer HIF peptide not containing cysteine is used, in order to rule out an involvement of the cysteine nitrosylation
-
-
?
bradykinin + 2-oxoglutarate + O2
4-hydroxyproline containing bradykinin
-
-
-
?
carboxymethylated collagen L-proline + 2-oxoglutarate + O2
carboxymethylated collagen-trans-4-hydroxy-L-proline + succinate + CO2
collagen + 2-oxoglutarate + O2
4-hydroxyproline containing collagen + succinate + CO2
-
-
-
?
DALTLLAPAAGDTIISLDYG + 2-oxoglutarate + O2
?
-
NODD peptide derived from native HIF-1alpha395-414
-
-
?
DALTLLAPAAGDTIISLFG + 2-oxoglutarate + O2
DALTLLA-((4R)-4-hydroxy-L-proline)-AAGDTIISLFG + succinate + CO2
-
-
-
?
dansyl-Gly-Phe-Pro-Gly-OEt + 2-oxoglutarate + O2
dansyl-Gly-Phe-4-hydroxy-L-Pro-Gly-OEt + succinate + CO2
-
-
-
-
?
dansyl-Gly-Phe-Pro-Gly-OEt + 2-oxoglutarate + O2
dansyl-Gly-Phe-trans-4-hydroxy-L-proline-Gly-OEt + succinate + CO2
-
-
-
-
?
DLDLEALAPYIPADDDFQL + 2-oxoglutarate + O2
?
-
CODD peptide derived from native HIF-1alpha556-574. PHD2 preferred CODD by 20fold over NODD
-
-
?
DLDLEMLAPAIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-AIPMDDDFQL + succinate + CO2
-
-
-
?
DLDLEMLAPAIPMDDDFQLRSFDQ + 2-oxoglutarate + O2
DLDLEMLAPAIPMDDDFQLRSFDQ trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
DLDLEMLAPGIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLAPGIPMDDDFQL trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
DLDLEMLAPYIPMD + 2-oxoglutarate + O2
DLDLEMLAPYIPMD trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
DLDLEMLAPYIPMDD + 2-oxoglutarate + O2
DLDLEMLAPYIPMDD trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
DLDLEMLAPYIPMDDDF + 2-oxoglutarate + O2
DLDLEMLAPYIPMDDDF trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
DLDLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLAPYIPMDDDFQL trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
DLDLEMLAPYIPMDDDFQLRSFDQ + 2-oxoglutarate + O2
DLDLEMLAPYIPMDDDFQLRSFDQ trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
DLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2
DLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
-
-
-
?
EMLAPYIPMDDDFQL + 2-oxoglutarate + O2
EMLAPYIPMDDDFQL trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
Glu-Gly-(Pro-Pro-Gly)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
Gly-Pro8 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
Gly-Val-Pro-Gly-Val + 2-oxoglutarate + O2
Gly-Val-4-hydroxyproline-Gly-Val + succinate + CO2
-
-
?
human procollagen-like (P-P-G)10 peptide L-proline + 2-oxoglutarate + O2
human procollagen-like (P-P-G)10 peptide trans-4-hydroxy-L-proline + succinate + CO2
Q81LZ8
4 different peptide sequences, anaerobic conditions
-
-
?
human procollagen-like (P-P-G)5 peptide L-proline + 2-oxoglutarate + O2
human procollagen-like (P-P-G)5 peptide trans-4-hydroxy-L-proline + succinate + CO2
Q81LZ8
5 different peptide sequences, anaerobic conditions
-
-
?
hypoxia-induced factor alpha oxygen-dependent degradation domain L-proline + 2-oxoglutarate + O2
hypoxia-induced factor alpha oxygen-dependent degradation domain L-4-hydroxyproline + succinate + CO2
-
-
in vitro hydroxylation of two proline residues, with preference for C-terminal proline
-
?
hypoxia-inducible factor alpha L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor alpha trans-4-hydroxy-L-proline + succinate + CO2
hypoxia-inducible factor L-proline + 2-oxoglutarate + O2
hypoxia inducible factor trans-4-hydroxy-L-proline + succinate + CO2
hypoxia-inducible factor L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
L-Ala-(L-Pro)4-Gly-L-Ile-L-Pro-Gly-L-Tyr-(L-Pro)2-L-Ala-(L-Pro)4-Gly-L-Val-Gly-(L-Pro)4-L-Gln-Gly L-proline + 2-oxoglutarate + O2
L-Ala-(L-Pro)4-Gly-L-Ile-L-Pro-Gly-L-Tyr-(L-Pro)2-L-Ala-(L-Pro)4-Gly-L-Val-Gly-(L-Pro)4-L-Gln-Gly trans-4-hydroxy-L-proline + succinate + CO2
-
-
peptide substrate representing proline-rich proteins expressed in the pharyngeal gland cells. 380% of the activity with (L-Pro-L-Glu-L-Pro-L-Pro-L-Ala)5 L-proline
-
?
L-Pro-L-Ala-L-Pro-L-Lys + 2-oxoglutarate + O2
L-Pro-L-Ala-L-Pro-L-Lys-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
L-Pro-L-Ile-(L-Pro)7-L-Leu-L-Pro-L-Gln-L-Asn-L-Leu-L-Ser-Gly-L-Ala-L-Pro L-proline + 2-oxoglutarate + O2
L-Pro-L-Ile-(L-Pro)7-L-Leu-L-Pro-L-Gln-L-Asn-L-Leu-L-Ser-Gly-L-Ala-L-Pro trans-4-hydroxy-L-proline + succinate + CO2
-
-
peptide substrate representing proline-rich proteins expressed in the pharyngeal gland cells. 610% of the activity with (L-Pro-L-Glu-L-Pro-L-Pro-L-Ala)5 L-proline
-
?
L-Pro-L-Pro-Gly + 2-oxoglutarate + O2
L-Pro-L-Pro-Gly-trans-4-hydroxy-L-proline + succinate + CO2
L-proline + 2-oxoglutarate + O2
4-hydroxyproline + succinate + CO2
LAPYIPMDDDFQL + 2-oxoglutarate + O2
LAPYIPMDDDFQL trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
Lys-Pro-Ala + 2-oxoglutarate + O2
Lys-4-hydroxyproline-Ala + succinate + CO2
-
recombinant enzyme
-
?
lysine hydroxylated protocollagen + 2-oxoglutarate + O2
lysine 4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
octa-L-proline + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
PEG-Gly-Tyr-4-fluoroproline-GlyOEt + 2-oxoglutarate + O2
?
-
-
-
-
?
peptidyl L-proline + 2-oxoglutarate + O2
peptidyl-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
poly L-proline + 2-oxoglutarate + O2
poly trans-4-hydroxy-L-proline + succinate + CO2
-
molecular weights of 5000 Da, 8000 Da and 32000 Da, respectively
-
-
?
poly(ethylene glycol)-Gly-L-Tyr-(2S)-4-thiaproline-Gly-OCH2CH2OH + 2-oxoglutarate + O2
poly(ethylene glycol)-Gly-L-Tyr-L-(2S,4R)-thiaoxoproline-Gly-OCH2CH2OH + ? + CO2
-
6% of the activity with L-prolyl peptide substrate
-
-
?
poly(ethylene glycol)-Gly-L-Tyr-L-(2S,4S)-4-fluoroproline-Gly-OCH2CH2OH + 2-oxoglutarate + O2
poly(ethylene glycol)-Gly-L-Tyr-L-(2S)-4-oxoproline-Gly-OCH2CH2OH + ? + CO2
-
26% of the activity with L-prolyl peptide substrate
-
-
?
poly(ethylene glycol)-Gly-L-Tyr-L-Pro-Gly-OCH2CH2OH + 2-oxoglutarate + O2
poly(ethylene glycol)-Gly-L-Tyr-L-(2S,4R)-4-hydroxy-Pro-Gly-OCH2CH2OH + succinate + CO2
-
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
poly(L-Pro) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
poly(L-proline) + 2-oxoglutarate + O2
poly trans-4-hydroxy-L-proline + succinate + CO2
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
poly(L-proline) + O2
?
-
substrate MW is 5000 kDa
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-(2S,4R)-4-hydroxy-L-proline + succinate + CO2
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
protocollagen type I L-proline + 2-oxoglutarate + O2
protocollagen type I-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
protocollagen type I L-proline+ 2-oxoglutarate + O2
protocollagen type I-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
Ser-Pro-Pro-Pro-Pro-Val-Ser-Pro-Pro-Pro-Val-Ser-Pro-Pro-Pro-Pro-Val + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
?
Ser-Pro-Pro-Pro-Val-Tyr-Lys-Ser-Pro-Pro-Pro-Pro-Val-Lys-His-Tyr-Ser-Pro-Pro-Pro-Val + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
?
SPPPPVSPPPVSPPPPV + 2-oxoglutarate + O2
trans-4-hydroxy-L-proline SPPPPVSPPPVSPPPPV + succinate + CO2
-
-
-
-
?
SPPPPVYKSPPPPVKHYSPPPV + 2-oxoglutarate + O2
trans-4-hydroxy-L-proline SPPPPVYKSPPPPVKHYSPPPV + succinate + CO2
-
-
-
-
?
tert-butyloxycarbonyl-Gly-Val-Pro-Gly-Val-OH + 2-oxoglutarate + O2
tert-butyloxycarbonyl-Gly-Val-Hyp-Gly-Val-OH + succinate + CO2
-
-
-
?
tert-butyloxycarbonyl-L-Pro-L-Pro-Gly + 2-oxoglutarate + O2
tert-butyloxycarbonyl-L-Pro-L-Pro-Gly-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
tert-butyloxycarbonyl-Pro-Pro-Ala-Pro-OH + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
tert-butyloxycarbonyl-Pro-Pro-Gln-Pro-OCH3 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
tert-butyloxycarbonyl-Pro-Pro-Gly-Pro + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
tert-butyloxycarbonyl-Pro-Pro-Gly-Pro-NHCH3 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
tert-butyloxycarbonyl-Pro-Pro-Gly-Pro-Pro-OH + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
tert-butyloxycarbonyl-Pro8 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
tert-butyloxycarbonyl-Val-Pro-Gly-Val-OH + 2-oxoglutarate + O2
tert-butyloxycarbonyl-Val-Hyp-Gly-Val-OH + succinate + CO2
-
-
-
?
additional information
?
-
(Gly-Ala-Pro)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
less than 10% relative activity with respect to (Gly-Pro-Ala)n
-
?
(Gly-Ala-Pro)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
active substrate
-
?
(Gly-Pro-Ala)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
the best substrate
-
?
(Gly-Pro-Ala)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
poor substrate
-
?
(Gly-Pro-Pro)10 + 2-oxoglutarate + O2
?
-
-
-
-
?
(Gly-Pro-Pro)10 + 2-oxoglutarate + O2
?
Q81LZ8
-
-
-
?
(L-Pro-L-Ala-L-Pro-L-Lys)3 + 2-oxoglutarate + O2
(L-Pro-L-Ala-L-Pro-L-Lys)3-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
r
(L-Pro-L-Ala-L-Pro-L-Lys)3 + 2-oxoglutarate + O2
(L-Pro-L-Ala-L-Pro-L-Lys)3-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
Paramecium bursaria Chlorella virus-1
-
-
-
-
r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
r
(L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(Pro-Ala-Pro-Lys)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
n: 3,10
-
?
(Pro-Ala-Pro-Lys)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
n: 1-10, recombinant enzyme, (Pro-Ala-Pro-Lys)10 is a particularly good substrate
-
?
(Pro-Glu-Pro-Pro-Ala)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
?
(Pro-Glu-Pro-Pro-Ala)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
recombinant enzyme
-
?
(Pro-Gly-Pro)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
active substrate
-
?
(Pro-Gly-Pro)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
active substrate
-
?
(Pro-Pro-Gly)10 + 2-oxoglutarate + O2
? + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)10 + 2-oxoglutarate + O2
? + succinate + CO2
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
(Pro-Pro-Gly)2 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)2 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)2 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)2 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
the enzyme acts in (Pro-Pro-Gly)10 preferentially on prolines in Y positions in the X-Y-Gly triplets
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
-
-
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 5,10, poor substrates
-
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
-
-
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
a low hydroxylation rate is found with denatured (Pro-Pro-Gly)10
-
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 20
n: 20, n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 20
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
structural requirement for proline hydroxylation in collagen and related peptides: supersecondary structure, consisting of PP-II followed by a beta-turn, as the conformational determinant for proline hydroxylation in nascent collagen and related substrates of the enzyme, in elastin peptides, the beta-structure appears to substitute for the PP-II structure
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
recombinant enzyme
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Ser-Pro-Lys-Pro-Pro)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
?
(Ser-Pro-Lys-Pro-Pro)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
recombinant enzyme, (Ser-Pro-Lys-Pro)5 is a particularly good substrate
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
uncoupled oxidative decarboxylation
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
uncoupled oxidative decarboxylation
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
uncoupled oxidative decarboxylation
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
carboxymethylated collagen L-proline + 2-oxoglutarate + O2
carboxymethylated collagen-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
carboxymethylated collagen L-proline + 2-oxoglutarate + O2
carboxymethylated collagen-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
Gly-Pro8 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
-
96% relative activity with respect to poly(L-proline) of MW 2000
-
?
Gly-Pro8 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
-
96% relative activity with respect to poly(L-proline) of MW 2000
-
?
His10-rSkp1A + ?
?
-
-
-
?
His10-rSkp1A + ?
?
-
-
-
?
hypoxia-inducible factor alpha L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor alpha trans-4-hydroxy-L-proline + succinate + CO2
isoform EGLN1 acts upon both the N-and the C-terminal oxygen-dependent degradation domain to target hypoxia-inducible factor alpha for proteasomal degradation
-
-
?
hypoxia-inducible factor alpha L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor alpha trans-4-hydroxy-L-proline + succinate + CO2
isoform EGLN2 acts upon both the N-and the C-terminal oxygen-dependent degradation domain to target hypoxia-inducible factor alpha for proteasomal degradation
-
-
?
hypoxia-inducible factor alpha L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor alpha trans-4-hydroxy-L-proline + succinate + CO2
isoform EGLN3 acts on the N-terminal oxygen-dependent degradation domain
-
-
?
hypoxia-inducible factor L-proline + 2-oxoglutarate + O2
hypoxia inducible factor trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor L-proline + 2-oxoglutarate + O2
hypoxia inducible factor trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
hypoxia-inducible factor L-proline + 2-oxoglutarate + O2
hypoxia inducible factor trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor L-proline + 2-oxoglutarate + O2
hypoxia inducible factor trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunit is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunit is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunti is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF, oxygen-dependent hydroxylation of proline residues in the alpha subunit of hypoxia-inducible transcription factor is central to the hypoxic response in animals. Prolyl hydroxylation of HIFalpha increases its binding to the von Hippel-Lindau protein, thus signaling for degradation via the ubiquitin-proteasome system
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF, the substrate prolyl-residue is bound in a specific conformation and that a significant structural change involving a mobile loop likely occurs concomitant with HIFalpha binding. PHD catalysis involves the mobile region that isolates the hydroxylation site and stabilizes the PHD2-Fe2+-2OG complex. The hydroxylation sites of both NODD and CODD of HIFalpha occur within a conserved LXXLAP motif. In the tPHD2-CODD structure, Leu559CODD, Leu562CODD, and Ala563CODD of the LXXLAP motif form part of the CODD310-helix and make hydrophobic interactions with tPHD2
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunit is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunti is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF
-
-
?
L-Pro-L-Pro-Gly + 2-oxoglutarate + O2
L-Pro-L-Pro-Gly-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
L-Pro-L-Pro-Gly + 2-oxoglutarate + O2
L-Pro-L-Pro-Gly-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
L-proline + 2-oxoglutarate + O2
4-hydroxyproline + succinate + CO2
-
2-oxoglutarate is essential for hydroxylation
-
?
L-proline + 2-oxoglutarate + O2
4-hydroxyproline + succinate + CO2
-
2-oxoglutarate is essential for hydroxylation
-
?
octa-L-proline + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
-
81.8% relative activity with respect to poly(L-proline) of MW 2000
-
?
octa-L-proline + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
-
81.8% relative activity with respect to poly(L-proline) of MW 2000
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
recombinant enzyme
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
do not serve as substrate, assayed with recombinant enzyme
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
MW 2000, 6000 and 12000
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
MW 2000, 6000 and 12000
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
MW 7000
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
Mr of poly(L-Pro) is about 5000
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
MW: 7000 and 44000
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
recombinant enzyme
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
Mr 30000-40000 Da, 15% of the activity with (L-Pro-L-Glu-L-Pro-L-Pro-L-Ala)5 L-proline
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
Mr 5000-10000 Da, 5, 24% of the activity with (L-Pro-L-Glu-L-Pro-L-Pro-L-Ala)5 L-proline
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
-
-
-
?
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
-
-
-
r
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
poly(L-proline) with Mr 10000-2000
-
-
r
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
poly(L-proline) with Mr 5000-1000
-
-
r
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
-
-
-
r
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
poly(L-proline) with Mr 40000
-
-
r
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
poly(L-proline) with Mr 13000
-
-
r
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
-
-
-
r
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-(2S,4R)-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-(2S,4R)-4-hydroxy-L-proline + succinate + CO2
-
prolyl 4-hydroxylase is a nonheme iron dioxygenase that catalyzes the posttranslational hydroxylation of (2S)-Pro residues in protocollagen strands
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
Q81LZ8
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
Q81LZ8
substrate binding and active site structure, overview
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
the enzyme preferentially recognizes the cis conformation of the prolyl peptide bond
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
key enzyme in collagen biosynthesis, catalyzes the conversion of selected prolyl residues to trans-hydroxyproline in nascent or completed pro-alpha chains of procollagen
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
the biological substrate for the enzyme is a proline residue in an appropriate sequence of a growing or newly synthesized polypeptide chain
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
key enzyme in collagen biosynthesis, catalyzes the conversion of selected prolyl residues to trans-hydroxyproline in nascent or completed pro-alpha chains of procollagen
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
the biological substrate for the enzyme is a proline residue in an appropriate sequence of a growing or newly synthesized polypeptide chain
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
acts on -Xaa-Pro-Gly triplets in collagen
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
P4H catalyzes the post-translational hydroxylation of proline residues in protocollagen strands, stabilizing the ensuing triple helix
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
high stringency for the iron-binding residues in the P4H active site, structure-function relationship, overview
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
PxGP (where x is not a proline) is the common motif of proline-rich peptide sequences that bind with high affinity to the enzyme (PSB-II)
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
the enzyme preferentially recognizes the cis conformation of the prolyl peptide bond
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
the binding affinity of 2-oxoglutarate to PcP4H1 is very low
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
the binding affinity of 2-oxoglutarate to PcP4H1 is very low
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
synthetic peptides
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
chelation to the enzyme-bound metal ion is important for proper binding of the substrate 2-oxoglutarate
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
no hydroxylation of free proline, minimum sequence required X-Pro-Gly, best substrates are those where Pro precedes Gly, which can be substituted by Ala or beta-alanine. The amino acid preceding Pro can be Pro, Ala, Leu, Arg, Val, Glu, but not Gly or Ser. Additionally the sequence, the conformation and the peptide chain length influence the rate of hydroxylation
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
the presence of 2-oxoglutarate is an absolute and highly specific requirement, the formation of 4-hydroxyproline is accompanied by a stoichiometric decarboxylation of 2-oxoglutarate, the oxygen of the hydroxyl group is derived from molecular oxygen, the other atom of the O2 molecule being incorporated into the succinate, the activated form of oxygen is probably superoxide
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
the presence of 2-oxoglutarate is an absolute and highly specific requirement, the formation of 4-hydroxyproline is accompanied by a stoichiometric decarboxylation of 2-oxoglutarate, the oxygen of the hydroxyl group is derived from molecular oxygen, the other atom of the O2 molecule being incorporated into the succinate, the activated form of oxygen is probably superoxide
-
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
no hydroxylation of free proline, minimum sequence required X-Pro-Gly, best substrates are those where Pro precedes Gly, which can be substituted by Ala or beta-alanine. The amino acid preceding Pro can be Pro, Ala, Leu, Arg, Val, Glu, but not Gly or Ser. Additionally the sequence, the conformation and the peptide chain length influence the rate of hydroxylation
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
the presence of 2-oxoglutarate is an absolute and highly specific requirement, the formation of 4-hydroxyproline is accompanied by a stoichiometric decarboxylation of 2-oxoglutarate, the oxygen of the hydroxyl group is derived from molecular oxygen, the other atom of the O2 molecule being incorporated into the succinate, the activated form of oxygen is probably superoxide
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
the presence of 2-oxoglutarate is an absolute and highly specific requirement, the formation of 4-hydroxyproline is accompanied by a stoichiometric decarboxylation of 2-oxoglutarate, the oxygen of the hydroxyl group is derived from molecular oxygen, the other atom of the O2 molecule being incorporated into the succinate, the activated form of oxygen is probably superoxide
-
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
2-oxoadipate can replace 2-oxoglutarate as cosubstrate
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
tert-butyloxycarbonyl-Pro8 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
-
91.4% relative activity with respect to poly(L-proline) of MW 2000
-
?
tert-butyloxycarbonyl-Pro8 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
-
91.4% relative activity with respect to poly(L-proline) of MW 2000
-
?
additional information
?
-
-
the enzyme preferentially hydroxylates proline residues preceding glycines in (X-Y-Gly)n peptides. Peptides representing the N- and C-terminal hydroxylation sites present in hypoxia-inducible transcription factor alpha also serve as substrates
-
-
?
additional information
?
-
the enzyme preferentially hydroxylates proline residues preceding glycines in (X-Y-Gly)n peptides. Peptides representing the N- and C-terminal hydroxylation sites present in hypoxia-inducible transcription factor alpha also serve as substrates
-
-
?
additional information
?
-
the enzyme preferentially hydroxylates proline residues preceding glycines in (X-Y-Gly)n peptides. Peptides representing the N- and C-terminal hydroxylation sites present in hypoxia-inducible transcription factor alpha also serve as substrates
-
-
?
additional information
?
-
the enzyme preferentially hydroxylates proline residues preceding glycines in (X-Y-Gly)n peptides. Peptides representing the N- and C-terminal hydroxylation sites present in hypoxia-inducible transcription factor alpha also serve as substrates
-
-
?
additional information
?
-
Q81LZ8
enzyme BaP4H recognizes and acts on peptidyl substrates but not free L-proline, using elements characteristic of an Fe(II)/2-oxoglutarate-dependent dioxygenases, substrate specifiicty analysis by mass spectrometry, fluorescence binding, x-ray crystallography, and docking experiments, overview. Enzyme BaP4H can hydroxylate unique peptidyl proline sites in collagen-derived peptides with asymmetric hydroxylation patterns. The cofactor-bound crystal structures of BaP4H reveal active site conformational changes that define open and closed forms and mimic 'ready' and 'product-released' states of the enzyme in the catalytic cycle. Free L-proline binds to Fe(II)-BaP4H, but the affinity is an order of magnitude lower than for the peptides. No activity with free L-proline
-
-
?
additional information
?
-
-
enzyme BaP4H recognizes and acts on peptidyl substrates but not free L-proline, using elements characteristic of an Fe(II)/2-oxoglutarate-dependent dioxygenases, substrate specifiicty analysis by mass spectrometry, fluorescence binding, x-ray crystallography, and docking experiments, overview. Enzyme BaP4H can hydroxylate unique peptidyl proline sites in collagen-derived peptides with asymmetric hydroxylation patterns. The cofactor-bound crystal structures of BaP4H reveal active site conformational changes that define open and closed forms and mimic 'ready' and 'product-released' states of the enzyme in the catalytic cycle. Free L-proline binds to Fe(II)-BaP4H, but the affinity is an order of magnitude lower than for the peptides. No activity with free L-proline
-
-
?
additional information
?
-
-
substrate and ligand binding structures, overview
-
-
?
additional information
?
-
-
no reaction with: free proline, prolyl peptides whose residues number is four or less
-
-
?
additional information
?
-
-
no reaction with: free proline, prolyl peptides whose residues number is four or less
-
-
?
additional information
?
-
-
protocollagen and triple-helical (Pro-Pro-Gly)10 do not serve as substrate. 2-oxoadipate, 2-oxosuccinate or 2-oxovalerate do not replace 2-oxoglutarate
-
-
?
additional information
?
-
-
substrate and ligand binding structures, overview
-
-
?
additional information
?
-
-
substrate specificity, overview. The substrate is bound in a lefthanded (poly)-L-proline type II conformation in a tunnel shaped by two loops, mode of binding does not depend on stacking interactions of the proline sidechains with aromatic residues, substrate binding structure, modelling, overview. Major conformational changes of the two peptide binding loops are predicted to be a key feature of the catalytic cycle. These conformational changes are probably triggered by the conformational switch of Tyr140, as induced by the hydroxylation of the proline residue
-
-
?
additional information
?
-
-
no reaction with: free proline, prolyl peptides whose residues number is four or less
-
-
?
additional information
?
-
-
P4H1 modifies Skp1, an adaptor of the SCF class of E3-Ub ligases
-
-
?
additional information
?
-
-
substrate and ligand binding structures, overview
-
-
?
additional information
?
-
-
the enzyme is specific for proline in the second position after glycine, the position in which the hydroxyproline in collagen is found. No reaction with: free proline, glycyl-L-prolyl-L-proline or poly-L-proline II with a molecular weight of about 15000
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
the presence of lysyl hydroxylase in the reaction mixture has no effect on the activity of the enzyme
-
-
?
additional information
?
-
-
characterization of the 2-oxoglutarate binding site of the enzyme, 2-oxosuccinate, 2-oxovalerate, 2-oxobutyrate, 3-oxoglutarate or pyridine 2,5-dicarboxylate do not replace 2-oxoglutarate as cosubstrates
-
-
?
additional information
?
-
-
in the absence of a peptidylproline substrate, the oxidative decarboxylation of 2-oxoglutarate by the enzyme is stoichiometrically coupled to the oxidation of ascorbate
-
-
?
additional information
?
-
-
no substrate: prolines in recombinant type I procollagen chains
-
-
?
additional information
?
-
-
HIF prolyl hydroxylases are related to the collagen prolyl hydroxylases, but form unusually stable complexes with their Fe2+ cofactor and 2-oxoglutarate cosubstrate
-
-
?
additional information
?
-
-
C-P4H catalyses proline hydroxylation of collagens in the X-Pro-Gly (X-P-G) triplets
-
-
?
additional information
?
-
-
the carboxy group of 2-oxoglutarate is bound by Lys493 in subunit alphaI, substrate and ligand binding structures, overview
-
-
?
additional information
?
-
-
the heat shock protein 90 (HSP90) co-chaperones p23 and FKBP38 interact via a conserved Pro-Xaa-Leu-Glu motif in these proteins with the N-terminal Myeloid Nervy and DEAF-1 (MYND)-type zinc finger of PHD2
-
-
?
additional information
?
-
prolyl-4-hydroxylase (P4H) is a non-heme iron hydroxylase that regio- and stereospecifically hydroxylates proline residues in a peptide chain into R-4-hydroxyproline. In P4H, a strong aliphatic C-H bond is activated, while thermodynamically much weaker aliphatic C-H groups, that is, at the C3 and C5 positions, are untouched
-
-
?
additional information
?
-
-
prolyl-4-hydroxylase (P4H) is a non-heme iron hydroxylase that regio- and stereospecifically hydroxylates proline residues in a peptide chain into R-4-hydroxyproline. In P4H, a strong aliphatic C-H bond is activated, while thermodynamically much weaker aliphatic C-H groups, that is, at the C3 and C5 positions, are untouched
-
-
?
additional information
?
-
-
no reaction with: free proline, prolyl peptides whose residues number is four or less
-
-
?
additional information
?
-
-
the enzyme clearly prefers X position proline to Y position proline in the sequences of (Gly-Pro-Ala)n versus (Gly-Ala-Pro)n
-
-
?
additional information
?
-
-
substrate and ligand binding structures, overview
-
-
?
additional information
?
-
-
no activity with poly-L-proline or the unhydroxylated decapeptide analog (Ala-Lys-Pro-Ser-Tyr-Pro-Pro-Thr-Tyr-Lys) of the polyphenolic protein
-
-
?
additional information
?
-
-
molecular mechanism of intracellular degradation of type I collagen in normal corneal endothelial cells, role of the enzyme and protein-disulfide isomerase, which is the beta subunit of the enzyme, during procollagen I biosynthesis
-
-
?
additional information
?
-
-
effect of substrate on activity
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
HPH isoforms are involved in infection of hosts and stress response
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
substrate and ligand binding structures, overview
-
-
?
additional information
?
-
-
the BH4 domain is required for the interaction of PHD3 with Bcl-2, PHD3 promotes apoptosis via its BH4 domain
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
2-oxoglutarate cannot be replaced by oxalylglycine, 2-oxopentanoate, 2-oxoadipate, pyruvate or 2-oxomalonate
-
-
?
additional information
?
-
-
2-oxoglutarate cannot be replaced by oxalylglycine, 2-oxopentanoate, 2-oxoadipate, pyruvate or 2-oxomalonate
-
-
?
additional information
?
-
-
proline or the dipeptides Ser-Pro or Ala-Pro do not serve as substrates
-
-
?
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(Pro-Pro-Gly)5
-
at concentrations higher than 0.56 mM, substrate inhibition observed
1,2,3-trihydroxybenzene
-
-
1,2-dihydroxybenzene
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
1,3-dihydroxybenzene
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
1,4-dihydrophenanthrolin-4-one-3-carboxylic acid
1,4,DPCA
1,4-dihydrophenanthroline-4-one-3-carboxylic acid
2,4-Dihydroxybenzoate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
2,4-pyridine dicarboxylate
-
-
2,5-Dihydroxybenzoate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
2,6-dihydroxybenzoate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
2,7,8-trihydroxyanthraquinone
-
50% inhibition at 0.047 mM, competitive inhibitor with respect to 2-oxoglutarate, non-competitive with regard to ascorbate, uncompetitive with regard to protocollagen. The inhibition is greatly enhanced in the absence of Fe2+, structural requirements for inhibition
2-Hydroxybenzoate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
2-oxoadipinate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
2-oxobutyrate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
2-oxoglutarate
-
at concentrations higher than 0.5 mM, decreases activity
2-oxovalerate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
3,4,5-Trihydroxybenzoate
-
-
3,4-dihydroxybenzoic acid
-
-
3,4-dihydroxycinnamate
-
competitive with respect to 2-oxoglutarate and ascorbate
3,4-dihydroxymandelate
-
competitive with respect to 2-oxoglutarate and ascorbate and noncompetitive with respect to Fe2+
3,4-dihydroxyphenyl acetate
IC50: 0.3 mM
3,4-Dihydroxyphenylacetate
3,4-Dihydroxyphenylpropionate
3,5-Dihydroxybenzoate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
3-carboxy-4-oxo-3,4-dihydro-1,10-phenanthroline
3-hydroxybutyrate
-
less than 10% inhibition
3-hydroxypyridine-2-carbonyl-glycine
3-oxoglutarate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
5-Azidopyridine-2-carboxylic acid
8-(N-butyl-N-ethylcarbamoyl)-1,4-dihydrophenanthrolin-4-one-3-carboxylic acid
8-hydroxyquinoline
-
inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
adipinate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
ADP-ribose
-
weak inhibitor
antimycin A
-
18% inhibition at 0.02 mM
benzene 1,2-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Benzene 1,3-dicarboxylate
Benzene 1,4-dicarboxylate
benzoate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
benzyloxycarbonyl-Phe-Opr-Gly-benzyl ester
Benzyloxycarbonyl-Phe-oxaproline-Gly-benzyl ester
citrate
-
competitive inhibition with respect to 2-oxoglutarate
CO2
-
5% inhibition at 3.6 mM, 35% inhibition at 7.2 mM and 75% inhibition at 12 mM
cobalt chloride
-
inhibition of PHDs blocks the response of mTORC1 to amino acids
Collagen
-
product inhibitor, noncompetitive with respect to all substrates of the reaction
concanavalin A
-
partially inhibits, when the enzyme is assayed in the absence of bovine serum albumin
-
CuCl2
-
0.4 mM, 67% inhibition
Cupferron
-
28% inhibition at 0.02 mM
deferoxamine mesylate
-
-
diethyl dicarbonate
-
98% inhibition at 1 mM
diethyldithiocarbamate
-
10% inhibition at 0.02 mM
Diethylenetriaminepentaacetic acid
-
inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
dimethyl oxalylglycine
-
DMOG, the effect is HIF-independent
dimethyloxallyl glycine
-
inhibition of PHDs blocks the response of mTORC1 to amino acids
dimethyloxalylalanine
-
50% inhibition in chicken embryo calvaria at 1 mM
dimethyloxalylglycine
-
50% inhibition in chicken embryo calvaria at 0.002 mM, inhibitor of hydroxyproline synthesis in embryonic chicken lung
epinephrine
-
competitive inhibition with respect to Fe2+
ethylpyridine-2,4-dicarboxylate
glutamyl-3,4-dehydroprolyl-bradykinin
-
H2O2
-
94% inhibition at 1 M, dissociation of the enzyme, 12% of the enzyme remains in the tetrameric form
Hg2+
-
causes a 20-30% fall in activity
HOE077
-
decrease in enzyme activity by 15%
isocitrate
-
competitive inhibition with respect to 2-oxoglutarate
L-galactono gamma-lactone
-
-
L-mimosine
-
50 mg/kg/day for 2 weeks
Lactate
-
less than 10% inhibition
levulinate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
malate
-
competitive inhibition with respect to 2-oxoglutarate
MgSO4
-
0.4 mM, 30% inhibition
Mn2+
-
causes a 20-30% fall in activity
MnSO4
-
0.4 mM, 62% inhibition
N,N'-diethylpyridine 2,4-dicarboxamide
N-((3-hydroxy-6-chloroquinolin-2-yl)carbonyl)glycine
-
-
N-(4-Azido-2-nitrophenyl)-glycyl-(Pro-Pro-Gly)5
N-Hydroxyethylenediaminetriacetic acid
-
inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
N-oxalylglycine
-
oxaloglycine derivative, inhibitor
N-[(6-chloro-3-hydroxyquinolin-2-yl)carbonyl]glycine
-
NiCl2
-
0.4 mM, 98% inhibition
oxaloacetate
-
competitive inhibition with respect to 2-oxoglutarate
oxalyl-beta-alanine
-
competitive inhibition with respect to 2-oxoglutarate
oxalylalanine
-
inhibits purified enzyme, competitive inhibition with respect to 2-oxoglutarate, 50% inhibition of microsomal enzyme at 0.123 mM
oxalylcystine
-
competitive inhibition with respect to 2-oxoglutarate
oxalylsarcosine
-
noncompetitive inhibition with respect to 2-oxoglutarate
Pd2+
-
strong irreversible inhibition, competitive with respect to Fe2+
phosphoribosyl adenosine monophosphate
-
46% inhibition at 25 nM, 87% inhibition at 50 nM
Poly(ADP-ribose)
-
near complete inhibition at 6 nM, the effect is noncompetitive with respect to the binding of the cofactors ascorbate and alpha-ketoglutarate or of the substrate
poly(L-Pro)
0.03 mM, 50% inhibition
poly-L-hydroxyproline
-
MW: 30000, inhibitory
-
potassium bromide
-
over 80% inhibition at 500 mM
potassium chloride
-
over 80% inhibition at 500 mM
potassium fluoride
-
over 90% inhibition at 500 mM
potassium iodide
-
over 80% inhibition at 500 mM
pyridine 2,3-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Pyridine 2,4-dicarboxylate
Pyridine 2,5-dicarboxylate
pyridine 2,6-dicarboxylate
-
competitive with respect to Fe2+ and noncompetitive with respect to 2-oxoglutarate
Pyridine 3,4-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Pyridine 3,5-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
pyridine 3-carboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Pyridine 4-carboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Pyridine-2,4-dicarboxylate
Pyridine-2,5-dicarboxylate
Ribosyl-ribosyl-adenine
-
43% inhibition at 25 nM, 85% inhibition at 50 nM
Ribosyl-ribosyl-hypoxanthine
-
40% inhibition at 25 nM, 86% inhibition at 50 nM
rosiglitazone
-
decrease in enzyme activity by 32.3%
S-nitroso-N-acetylpenicillamine
-
hyperoxia attenuates the inhibitory effect of NO on HIF-1alpha prolyl hydroxylation
S-nitrosoglutathione
-
hyperoxia attenuates the inhibitory effect of NO on HIF-1alpha prolyl hydroxylation
Salicylyl hydroxamate
-
-
sodium bromide
-
over 80% inhibition at 500 mM
sodium chloride
-
over 80% inhibition at 500 mM
sodium iodide
-
over 90% inhibition at 500 mM
sodium pyrocatechol disulfonate
-
98-100% inhibition at 0.1 mM
trifluorothienylbutanedione
-
48% inhibition at 0.05 mM
ZnSO4
-
0.4 mM, 84% inhibition
(Gly-Pro-Gly)n
-
competitive inhibitors with respect to the polypeptide substrate
(Gly-Pro-Gly)n
-
competitive inhibitors with respect to the polypeptide substrate
(Pro-Ala-Gly)n
-
competitive inhibitors with respect to the polypeptide substrate
(Pro-Ala-Gly)n
-
competitive inhibitors with respect to the polypeptide substrate
1,10-phenanthroline
-
-
1,10-phenanthroline
-
inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
1,10-phenanthroline
-
91% inhibition at 0.02 mM
1,4-dihydrophenanthroline-4-one-3-carboxylic acid
-
purified enzyme, competitive inhibitor of 2-oxoglutarate
1,4-dihydrophenanthroline-4-one-3-carboxylic acid
-
potent competitive inhibitor of collagen hydroxylation in the oestradiol-stimulated uterus in vivo
2,2'-dipyridyl
-
-
2,2'-dipyridyl
-
50% inhibition at 0.06 mM
2,2'-dipyridyl
-
inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
2,2'-dipyridyl
-
87% inhibition at 0.02 mM
2,3-Dihydroxybenzoate
-
-
2,3-Dihydroxybenzoate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
2,3-Dihydroxybenzoate
-
-
2-oxosuccinate
-
i.e. oxaloacetate
2-oxosuccinate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+; i.e. oxaloacetate
2-oxosuccinate
-
i.e. oxaloacetate
3,4-dihydroxybenzoate
-
-
3,4-dihydroxybenzoate
-
-
3,4-dihydroxybenzoate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
3,4-dihydroxybenzoate
-
-
3,4-dihydroxybenzoate
-
-
3,4-dihydroxybenzoate
-
-
3,4-Dihydroxyphenylacetate
-
-
3,4-Dihydroxyphenylacetate
-
competitive with respect to 2-oxoglutarate and ascorbate, noncompetitive with respect to Fe2+
3,4-Dihydroxyphenylacetate
-
-
3,4-Dihydroxyphenylacetate
-
-
3,4-Dihydroxyphenylacetate
-
-
3,4-Dihydroxyphenylacetate
-
-
3,4-Dihydroxyphenylacetate
-
-
3,4-Dihydroxyphenylpropionate
-
competitive with respect to 2-oxoglutarate and ascorbate
3,4-Dihydroxyphenylpropionate
-
-
3,4-Dihydroxyphenylpropionate
-
-
3,4-Dihydroxyphenylpropionate
-
-
3,4-Dihydroxyphenylpropionate
-
-
3-carboxy-4-oxo-3,4-dihydro-1,10-phenanthroline
-
3-carboxy-4-oxo-3,4-dihydro-1,10-phenanthroline
-
-
3-hydroxypyridine-2-carbonyl-glycine
-
3-hydroxypyridine-2-carbonyl-glycine
-
-
4-hydroxybenzoate
-
-
4-hydroxybenzoate
-
competitive with respect to 2-oxoglutarate, and noncompetitive with respect to ascorbate
4-oxo-5,6-epoxyhexanoate
-
Caenorhabditis elegans exposed to the esterified epoxy ketone displays the phenotype of a worm lacking P4H
4-oxo-5,6-epoxyhexanoate
-
-
5-Azidopyridine-2-carboxylic acid
-
incorporated in the alpha subunit of the enzyme, complete inactivation of the enzyme by incorporation of 2 mol of photoaffinity label per mol of tetramer
5-Azidopyridine-2-carboxylic acid
-
-
8-(N-butyl-N-ethylcarbamoyl)-1,4-dihydrophenanthrolin-4-one-3-carboxylic acid
-
purified enzyme, competitive inhibitor of 2-oxoglutarate
8-(N-butyl-N-ethylcarbamoyl)-1,4-dihydrophenanthrolin-4-one-3-carboxylic acid
-
potent competitive inhibitor of collagen hydroxylation in the oestradiol-stimulated uterus in vivo
alpha,alpha'-dipyridyl
-
an Fe2+ chelator
alpha,alpha'-dipyridyl
-
an Fe2+ chelator
alpha,alpha'-dipyridyl
-
an Fe2+ chelator
alpha,alpha'-dipyridyl
-
an Fe2+ chelator
alpha,alpha'-dipyridyl
-
an Fe2+ chelator
alpha,alpha'-dipyridyl
-
5 mM, potent inhibitor
alpha,alpha'-dipyridyl
-
an Fe2+ chelator
ascorbate
-
at high concentrations
ascorbate
-
the inhibition may result from competition for binding at the 2-oxoacid binding site between 2-oxoglutarate and L-ascorbate
Benzene 1,3-dicarboxylate
-
-
Benzene 1,3-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Benzene 1,4-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Benzene 1,4-dicarboxylate
-
competitive inhibition with respect to ascorbate
benzyloxycarbonyl-Phe-Opr-Gly-benzyl ester
-
50% inactivation in 1 h at 0.0008 mM, the most effective inhibitor within oxaproline peptides
benzyloxycarbonyl-Phe-Opr-Gly-benzyl ester
-
50% inactivation in 1 h at 0.0008 mM, the most effective inhibitor within oxaproline peptides
Benzyloxycarbonyl-Phe-oxaproline-Gly-benzyl ester
-
-
Benzyloxycarbonyl-Phe-oxaproline-Gly-benzyl ester
-
-
Beta-lactam antibiotics
-
-
Beta-lactam antibiotics
-
-
bradykinin analogs
-
especially those in which the proline in the -X-Pro-Gly- triplet is replaced by certain proline analogues, the addition of a glutamyl residue to the N-terminal end of 3,4-dehydroprolyl- or trans-4-hydroxyprolyl-bradykinin considerably increases their effectiveness
-
bradykinin analogs
-
especially those in which the proline in the -X-Pro-Gly- triplet is replaced by certain proline analogues, the addition of a glutamyl residue to the N-terminal end of 3,4-dehydroprolyl- or trans-4-hydroxyprolyl-bradykinin considerably increases their effectiveness
-
catechol analogues
-
inhibitor of the reaction due in part to the chelation of Fe2+
-
catechol analogues
-
inhibitor of the reaction due in part to the chelation of Fe2+
-
Cd2+
Q81LZ8
the binding of Cd2+ induces a conformational change in the enzyme structure compared to the wild-type enzyme, overview
Cd2+
-
competitive versus Fe2+
Cd2+
-
competitive versus Fe2+
Cd2+
-
competitive versus Fe2+
Cd2+
-
competitive versus Fe2+
Cd2+
-
competitive versus Fe2+
Cd2+
-
competitive versus Fe2+
ciclopirox olamine
-
an Fe2+ chelator
ciclopirox olamine
-
an Fe2+ chelator
ciclopirox olamine
-
an Fe2+ chelator
ciclopirox olamine
-
an Fe2+ chelator
ciclopirox olamine
-
an Fe2+ chelator
ciclopirox olamine
-
an Fe2+ chelator
Co2+
Q81LZ8
active site binding structure analysis, in both Co(II)-bound structures, in addition to the catalytic triad residues and 2-oxoglutarate or, malonate that coordinate cobalt, the remaining coordinate sites are occupied by water molecules thus forming a six-coordinate cobalt complex
Co2+
-
competitive versus Fe2+
Co2+
-
competitive versus Fe2+
Co2+
-
competitive versus Fe2+
Co2+
-
competitive versus Fe2+
Co2+
-
competitive versus Fe2+
Co2+
-
competitive versus Fe2+
Co2+
-
complete inhibition
CoCl2
IC50: 0.00025 mM
CoCl2
-
0.4 mM, complete inhibition
Coumalic acid
-
-
Coumalic acid
-
i.e. 2-oxo-1,2H-pyran-5-carboxylic acid
Coumalic acid
-
competitive inhibitor, potential syncatalytic inhibitor, time-dependent inactivation, increasing concentrations of Fe2+ enhance the inactivation; i.e. 2-oxo-1,2H-pyran-5-carboxylic acid
Coumalic acid
-
i.e. 2-oxo-1,2H-pyran-5-carboxylic acid
Coumalic acid
-
competitive inhibitor, potential syncatalytic inhibitor, time-dependent inactivation, increasing concentrations of Fe2+ enhance the inactivation; i.e. 2-oxo-1,2H-pyran-5-carboxylic acid
Cu2+
-
-
Cu2+
-
causes a 20-30% fall in activity
daunorubicin
-
-
daunorubicin
-
irreversible inhibitor, 50% inhibition after 1 h at 0.06 mM, effect dependent on the presence of iron ions
daunorubicin
-
irreversible inhibitor, 50% inhibition after 1 h at 0.06 mM, effect dependent on the presence of iron ions
desferrioxamine
-
an Fe2+ chelator
desferrioxamine
-
an Fe2+ chelator
desferrioxamine
-
an Fe2+ chelator
desferrioxamine
-
an Fe2+ chelator
desferrioxamine
-
an Fe2+ chelator
desferrioxamine
-
an Fe2+ chelator
dilantin
-
inhibitor of the reaction due in part to the chelation of Fe2+
dilantin
-
inhibitor of the reaction due in part to the chelation of Fe2+
dithiothreitol
-
95-100% inhibition at 0.45 mM
dithiothreitol
-
powerful inhibitor at 1 mM
doxorubicin
-
-
doxorubicin
-
irreversible inhibitor, 50% inhibition after 1 h at 0.06 mM, effect dependent on the presence of iron ions
doxorubicin
-
irreversible inhibitor, 50% inhibition after 1 h at 0.06 mM, effect dependent on the presence of iron ions
doxorubicin
-
not inhibitory at concentration up to 0.5 mM
EDTA
-
98-100% inhibition at 0.01 mM
EDTA
-
0.4 mM, 74% inhibition
EDTA
-
50% inhibition at 0.15 mM
EDTA
-
inhibits at a concentration higher than the Fe2+ concentration in the reaction mixture
EDTA
-
64% inhibition at 0.02 mM
ethylpyridine-2,4-dicarboxylate
-
-
ethylpyridine-2,4-dicarboxylate
-
-
Fe2+
-
inhibitory at high concentrations
Fe2+
-
inhibitory at a concentration higher than 0.5 mM
fumarate
-
competitive inhibition with respect to 2-oxoglutarate
gelatin
-
commercial, inhibitor
-
gelatin
-
commercial, inhibitor
-
gelatin
-
commercial, inhibitor
-
glutamyl-3,4-dehydroprolyl-bradykinin
-
-
-
glutamyl-3,4-dehydroprolyl-bradykinin
-
-
-
Glutarate
-
-
Glutarate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
hydralazine
-
inhibitor of the reaction due in part to the chelation of Fe2+
hydralazine
-
inhibitor of the reaction due in part to the chelation of Fe2+
Ketomalonate
-
100% inhibition at 1 mM, acts by chelating ferrous ion rather than by competing with alpha-ketoglutarate
Ketomalonate
-
100% inhibition at 1 mM, acts by chelating ferrous ion rather than by competing with alpha-ketoglutarate
Ketomalonate
-
100% inhibition at 1 mM, acts by chelating ferrous ion rather than by competing with alpha-ketoglutarate
malonate
Q81LZ8
active site binding structure analysis
malonate
-
19% inhibition at 1 mM
malonate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
malonate
-
19% inhibition at 1 mM
malonate
-
19% inhibition at 1 mM
N,N'-diethylpyridine 2,4-dicarboxamide
-
-
N,N'-diethylpyridine 2,4-dicarboxamide
-
-
N-(4-Azido-2-nitrophenyl)-glycyl-(Pro-Pro-Gly)5
-
loss of enzyme activity with (Pro-Pro-Gly)5 as a substrate upon photoaffinity labeling
N-(4-Azido-2-nitrophenyl)-glycyl-(Pro-Pro-Gly)5
-
-
NaCl
-
more than 0.3 M
Ni2+
-
competitive versus Fe2+
Ni2+
-
competitive versus Fe2+
Ni2+
-
competitive versus Fe2+
Ni2+
-
competitive versus Fe2+
Ni2+
-
competitive versus Fe2+
Ni2+
-
competitive versus Fe2+
nitroblue tetrazolium
-
is capable of scavenging superoxide, competitive inhibitor with respect to O2
nitroblue tetrazolium
-
competitive inhibition with respect to O2
nitroblue tetrazolium
-
is capable of scavenging superoxide, competitive inhibitor with respect to O2
oxalate
-
34% inhibition at 1 mM
oxalate
-
34% inhibition at 1 mM
oxalate
-
34% inhibition at 1 mM
oxalylglycine
-
inhibits purified enzyme, competitive inhibition with respect to 2-oxoglutarate, 50% inhibition of microsomal enzyme at 0.023 mM
phenanthrolines
-
potent competitive inhibitors inhibitory of purified enzyme; potent competitive inhibitors of collagen hydroxylation in embryonic tendon cells in vitro
-
phenanthrolines
-
potent competitive inhibitors of collagen hydroxylation in foreskin fibroblasts in vitro
-
poly(L-proline)
-
not inhibitory
-
poly(L-proline)
-
MW: 7000 and 44000
-
poly(L-proline)
-
competitive inhibitors with respect to the polypeptide substrate, the inhibition increases with chain length
-
poly(L-proline)
-
competitive inhibitor with respect to the polypeptide substrate and uncompetitive with respect to Fe2+ and 2-oxoglutarate
-
poly(L-proline)
-
competitive inhibitors with respect to the polypeptide substrate, the inhibition increases with chain length
-
poly(L-proline)
-
inhibitory, type I enzyme tetramer, MW: 7000 and 44000
-
poly(L-proline)
type I und II enzyme
-
poly(L-proline)
-
MW: 7000 and 44000
-
poly(L-proline)
-
inhibitor, recombinant type II enzyme tetramer, MW: 7000 and 44000
-
poly(L-proline)
-
competitive inhibition
-
propyl gallate
-
100% inhibition at 2 mM
propyl gallate
-
100% inhibition at 2 mM
propyl gallate
-
100% inhibition at 2 mM
Pyridine 2,4-dicarboxylate
-
not inhibitory
Pyridine 2,4-dicarboxylate
-
recombinant enzyme, competitive inhibitor with respect to Fe2+ and 2-oxoglutarate
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Pyridine 2,4-dicarboxylate
-
uncompetitive inhibition with respect to ascorbate
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
inhibits wild-type enzyme and enzyme tetramer containing the histidine 501 to serine mutant alpha subunit
Pyridine 2,4-dicarboxylate
-
inhibitory, type I enzyme tetramer
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
inhibitory, recombinant type II enzyme tetramer
Pyridine 2,4-dicarboxylate
-
effective inhibitor
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,5-dicarboxylate
-
-
Pyridine 2,5-dicarboxylate
-
-
Pyridine 2,5-dicarboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
Pyridine 2,5-dicarboxylate
-
uncompetitive inhibition with respect to ascorbate
Pyridine 2,5-dicarboxylate
-
-
Pyridine 2,5-dicarboxylate
-
-
Pyridine 2,5-dicarboxylate
-
-
pyridine 2-carboxylate
-
-
pyridine 2-carboxylate
-
-
pyridine 2-carboxylate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
pyridine 2-carboxylate
-
uncompetitive inhibition with respect to ascorbate
Pyridine-2,4-dicarboxylate
-
competitive inhibition
Pyridine-2,4-dicarboxylate
-
-
Pyridine-2,4-dicarboxylate
-
Pyridine-2,4-dicarboxylate
0.011 mM, 50% inhibition
Pyridine-2,5-dicarboxylate
-
competitive inhibition
Pyridine-2,5-dicarboxylate
-
-
Pyridine-2,5-dicarboxylate
0.007 mM, 50% inhibition
pyruvate
-
-
pyruvate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
pyruvate
-
competitive inhibition with respect to 2-oxoglutarate
succinate
-
11.5% inhibition at 0.5 mM and 38.3% inhibition at 3 mM
succinate
-
51% inhibition at 1 mM
succinate
-
competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+
succinate
-
51% inhibition at 1 mM
succinate
-
product inhibition
succinate
-
51% inhibition at 1 mM
tetracyclin
-
inhibitor of the reaction due in part to the chelation of Fe2+
tetracyclin
-
inhibitor of the reaction due in part to the chelation of Fe2+
Zn2+
-
recombinant enzyme, competitive inhibition with respect to Fe2+ and 2-oxoglutarate
Zn2+
-
competitive versus Fe2+
Zn2+
-
comptitive versus Fe2+
Zn2+
-
Zn2+ is bound at each of the four active sites, binding structure, overview
Zn2+
-
competitive versus Fe2+
Zn2+
-
competitive inhibition with respect to Fe2+, non-competitive with respect to the polypeptide substrate and 2-oxoglutarate
Zn2+
-
competitive versus Fe2+
Zn2+
-
competitive versus Fe2+
Zn2+
-
competitive versus Fe2+
Zn2+
-
complete inhibition
additional information
-
high concentrations of salts are inhibitory
-
additional information
-
synthetic peptides containing the non-physiologic amino acid 5-oxaproline in the sequence R1-Xaa-oxaproline-Gly-OR2 are specific syncatalytic inactivators, noncompetitive inhibition with respect to peptide substrate and ascorbate, compounds with aromatic substituents R1 and R2 are particularly effective when compared with those with an aliphatic group, inactivation is only observed in the presence of Fe2+ and 2-oxoglutarate
-
additional information
-
the synthesis and degradation of ADP-ribose moieties may possibly regulate prolyl hydroxylase activity in vivo
-
additional information
-
inhibition of the purified enzyme and of collagen hydroxylation in embryonic tendon fibroblast by novel phenanthrolines, structure-activity relationships
-
additional information
-
synthetic peptides containing the non-physiologic amino acid 5-oxaproline in the sequence R1-Xaa-oxaproline-Gly-OR2 are specific syncatalytic inactivators, noncompetitive inhibition with respect to peptide substrate and ascorbate, compounds with aromatic substituents R1 and R2 are particularly effective when compared with those with an aliphatic group, inactivation is only observed in the presence of Fe2+ and 2-oxoglutarate
-
additional information
-
inhibition of the secretion of procollagen in foreskin fibroblasts by novel phenanthrolines, structure-activity relationships
-
additional information
-
high concentrations of salts are inhibitory
-
additional information
-
hypoxia inhibits the enzyme
-
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