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Enzyme Nomenclature
Information on EC 1.14.11.35 - 1-deoxypentalenic acid 11beta-hydroxylase
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1.14.11.35 1-deoxypentalenic acid 11beta-hydroxylaseIUBMB Comments
The enzyme requires Fe(II) and ascorbate. Isolated from the bacterium Streptomyces avermitilis. Part of the pathway for pentalenolactone biosynthesis.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
pntH
-
-
-
-
ptlH
sav2991
-
-
-
-
ptlH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-deoxypentalenate + 2-oxoglutarate + O2 = 1-deoxy-11beta-hydroxypentalenate + succinate + CO2
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
1-deoxypentalenic acid,2-oxoglutarate:oxygen oxidoreductase
The enzyme requires Fe(II) and ascorbate. Isolated from the bacterium Streptomyces avermitilis. Part of the pathway for pentalenolactone biosynthesis.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+/-)-1-deoxypentalenic acid + O2
11beta-hydroxy-1-deoxypentalenic acid + succinate + CO2
-
-
-
?
additional information
?
-
no substrate: (+/-)-pentalenene, (+/-)-pentalen-13-ol
-
-
?
additional information
?
-
no substrate: ent-1-deoxypentalenic acid
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
non-heme iron, alpha-ketoglutarate-dependent hydroxylase
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.57
(+/-)-1-deoxypentalenic acid
pH 6.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.2
(+/-)-1-deoxypentalenic acid
pH 6.0, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PTLH_STRAW
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
285
0
32264
Swiss-Prot
-
A0A2P5VM21_9PROT
337
0
38597
TrEMBL
-
A0A1J5STZ1_9ZZZZ
275
0
30793
TrEMBL
other Location (Reliability: 1)
A0A517T2S2_9BACT
255
0
28824
TrEMBL
-
A0A2S6RLD0_9PROT
348
0
39235
TrEMBL
-
A0A517ME00_9BACT
261
0
29435
TrEMBL
-
A0A1V5FR86_9BACT
289
0
33655
TrEMBL
-
A0A2S6RKK2_9PROT
280
0
32221
TrEMBL
-
A0A5C6C723_9BACT
257
0
29320
TrEMBL
-
A0A1V5FGU3_9BACT
305
0
34991
TrEMBL
-
A0A347W879_9PROT
277
0
30781
TrEMBL
-
A0A517N4D6_9BACT
256
0
29399
TrEMBL
-
A0A1V5RSS5_9CHLR
312
0
35952
TrEMBL
-
A0A1V5FRU4_9BACT
282
0
32669
TrEMBL
-
A0A2Z2NRI0_9GAMM
291
0
33017
TrEMBL
-
A0A1V5RZ23_9CHLR
302
0
34013
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexes with the cofactors iron, alpha-ketoglutarate, and the nonreactive enantiomer of the substrate, ent-1-deoxypentalenic acid, in four different crystal forms to up to 1.31 A resolution. The overall structure of PtlH forms a double-stranded barrel helix fold and the cofactor-binding site for iron and alpha-keto-glutarate is similar to other double-stranded barrel helix fold enzymes. Binding of the substrate enantiomer induces a reorganization of the monoclinic crystal lattice leading to a disorder-order transition of a C-terminal alpha-helix. The newly formed helix blocks the major access to the active site and effectively traps the bound substrate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
You, Z.; Omura, S.; Ikeda, H.; Cane, D.E.
Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlH, a non-heme iron dioxygenase of Streptomyces avermitilis
J. Am. Chem. Soc.
128
6566-6567
2006
Streptomyces avermitilis (Q82IZ1)
brenda
You, Z.; Omura, S.; Ikeda, H.; Cane, D.E.; Jogl, G.
Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis
J. Biol. Chem.
282
36552-36560
2007
Streptomyces avermitilis (Q82IZ1)
brenda
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