Any feedback?
Information on EC 3.4.23.42 - thermopsin
for references in articles please use BRENDA:EC3.4.23.42Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.23.42 thermopsinSpecify your search results
Word Map
- 3.4.23.42
- hallux
-
metatarsophalangeal
- valgus
- acidocaldarius
-
rigidus
-
forefoot
-
dorsiflexion
-
nonunion
-
screw
-
pepstatin-insensitive
-
intermetatarsal
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
Reaction Schemes
similar in specificity to pepsin A preferring bulky hydrophobic amino acids in P1 and P1'
Synonyms
mtp-1, thermopsin, ssmtp, sso1175, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.4.99.43
-
-
formerly
-
MTP-1
SsMTP
SSO1175
SSO2045
Sulfolobus solfataricus multidomain thermopsin-like protease
additional information
-
the enzyme belongs to the A5 peptidase family
SsMTP
a multi-domain thermopsin-like protease containing the catalytic domain followed by two distinct domains, PKD and Y_Y_Y, which are usually involved in a range of protein-protein interactions among the extracellular proteins. The characteristic active site amino acid sequence for aspartic proteases, Asp Thr Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in SsMTP as in Sulfolobus acidocaldarius thermopsin, suggesting that different catalytic mechanisms are employed by these proteases
SsMTP
a multi-domain thermopsin-like protease containing the catalytic domain followed by two distinct domains, PKD and Y_Y_Y, which are usually involved in a range of protein-protein interactions among the extracellular proteins. The characteristic active site amino acid sequence for aspartic proteases, Asp Thr Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in SsMTP as in Sulfolobus acidocaldarius thermopsin, suggesting that different catalytic mechanisms are employed by these proteases
-
Sulfolobus solfataricus multidomain thermopsin-like protease
-
Sulfolobus solfataricus multidomain thermopsin-like protease
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
similar in specificity to pepsin A preferring bulky hydrophobic amino acids in P1 and P1'
prefers large hydrophobic residues at both sides of the scissile bond
-
similar in specificity to pepsin A preferring bulky hydrophobic amino acids in P1 and P1'
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
126125-05-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLCGSHL + VEAL + YLVCGERGF + L-Phe + YTPKA
-
substrate insulin B chain
-
-
?
Lys-Pro-Ala-Glu-Phe-Nph-Ala-Leu + H2O
Lys-Pro-Ala-Glu-Phe + Nph-Ala-Leu
-
synthetic chromogenic substrate
-
-
?
oxidized insulin B + H2O
?
-
following bonds are hydrolyzed: Leu-Val, Leu-Tyr, Phe-Phe, Phe-Tyr, Tyr-Thr
-
-
?
Bovine insulin B-chain + H2O
?
the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr
-
-
?
Bovine insulin B-chain + H2O
?
the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr
-
-
?
Hemoglobin + H2O
?
the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr
-
-
?
Hemoglobin + H2O
?
the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr
-
-
?
insulin B chain + H2O
?
-
cleavage sites are Val-Asn, Cys-Gly, Leu-Tyr, Glu-Arg, Gly-Phe and Pro-Lys
-
?
insulin B chain + H2O
?
-
cleavage sites are Val-Asn, Cys-Gly, Leu-Tyr, Glu-Arg, Gly-Phe and Pro-Lys
-
?
insulin B chain + H2O
?
-
-
cleavage sites are Val-Asn, Cys-Gly, Leu-Tyr, Glu-Arg, Gly-Phe and Pro-Lys
-
?
Lys-Pro-Ala-Glu-Phe-(4-nitro)Phe-Ala-Leu + H2O
Lys-Pro-Ala-Glu-Phe + (4-nitro)Phe-Ala-Leu
-
-
-
?
Lys-Pro-Ala-Glu-Phe-(4-nitro)Phe-Ala-Leu + H2O
Lys-Pro-Ala-Glu-Phe + (4-nitro)Phe-Ala-Leu
-
-
-
?
N-CBZ-glycine 4-nitrophenyl ester + H2O
N-CBZ-Gly + 4-nitrophenol
-
-
-
?
N-CBZ-glycine 4-nitrophenyl ester + H2O
N-CBZ-Gly + 4-nitrophenol
-
-
-
?
N-CBZ-glycine 4-nitrophenyl ester + H2O
N-CBZ-Gly + 4-nitrophenol
-
-
-
-
?
additional information
?
-
the enzyme shows no sequence similarity to aspartic proteases of the pepsin family or to pepstatin-insensitive acid protease. The characteristic active site amino acid sequence for aspartic proteases, Asp-Thr-Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in SsMTP from Sulfolobus solfataricus as in Sulfolobus acidocaldarius thermopsin, suggesting that different catalytic mechanisms are employed by these proteases
-
-
?
additional information
?
-
-
the enzyme shows no sequence similarity to aspartic proteases of the pepsin family or to pepstatin-insensitive acid protease. The characteristic active site amino acid sequence for aspartic proteases, Asp-Thr-Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in SsMTP from Sulfolobus solfataricus as in Sulfolobus acidocaldarius thermopsin, suggesting that different catalytic mechanisms are employed by these proteases
-
-
?
additional information
?
-
the enzyme shows no sequence similarity to aspartic proteases of the pepsin family or to pepstatin-insensitive acid protease. The characteristic active site amino acid sequence for aspartic proteases, Asp-Thr-Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in SsMTP from Sulfolobus solfataricus as in Sulfolobus acidocaldarius thermopsin, suggesting that different catalytic mechanisms are employed by these proteases
-
-
?
additional information
?
-
-
the enzyme shows a broad protein substrate specificity, it is involved in supply of nutrients from protein substrates
-
-
?
additional information
?
-
-
the enzyme shows a broad protein substrate specificity
-
-
?
additional information
?
-
-
The characteristic active site amino acid sequence for aspartic proteases, Asp Thr Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in thermopsin from Sulfolobus acidocaldarius, suggesting that a different catalytic mechanisms is employed.
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
the enzyme shows a broad protein substrate specificity, it is involved in supply of nutrients from protein substrates
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
not inhibitory: phenylmethylsulfonyl fluoride, EDTA, or pepstatin
-
additional information
-
not inhibitory: phenylmethylsulfonyl fluoride, EDTA, or pepstatin
-
additional information
-
no inhibition by iodoacetate and 4-chloromercuribenzoate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Arthralgia
First metatarsophalangeal arthroscopy in patients with post-traumatic hallux valgus.
Arthritis
Combination of first metatarsophalangeal joint arthrodesis and proximal correction for severe hallux valgus deformity.
Arthritis
Computer assisted planning and custom-made surgical guide for malunited pronation deformity after first metatarsophalangeal joint arthrodesis in rheumatoid arthritis: A case report.
Congenital Abnormalities
Combination of first metatarsophalangeal joint arthrodesis and proximal correction for severe hallux valgus deformity.
Congenital Abnormalities
Computer assisted planning and custom-made surgical guide for malunited pronation deformity after first metatarsophalangeal joint arthrodesis in rheumatoid arthritis: A case report.
Flatfoot
Flexor Hallucis Longus tendon rupture in RA-patients is associated with MTP 1 damage and pes planus.
Gout
Additive value for ultrasonographic signal in a screening algorithm for patients presenting with acute mono-/oligoarthritis in whom gout is suspected.
Hallux Valgus
Combination of first metatarsophalangeal joint arthrodesis and proximal correction for severe hallux valgus deformity.
Hallux Valgus
Computer assisted planning and custom-made surgical guide for malunited pronation deformity after first metatarsophalangeal joint arthrodesis in rheumatoid arthritis: A case report.
Hallux Valgus
First metatarsophalangeal arthroscopy in patients with post-traumatic hallux valgus.
Hallux Valgus
Severe Hallux Valgus Angle Attended With High Incidence of Nonunion in Arthrodesis of the First Metatarsophalangeal Joint: A Follow-Up Study.
Synovitis
MR-detected features of inflammation and erosions occur in symptom-free persons from the general population.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 12
-
activity range, highest activity at pH 1.0- pH 5.0, substrate hemoglobin
1.3 - 3.7
pH 1.3: about 60% of maximal activity, pH 3.7: about 55% of maximal activity
2 - 4
pH 2.0: optimum, pH 4.0: about 50% of maximal activity, no activity detectable at pH 6.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
90
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 100
-
activity range, substrate hemoglobin, slow activity increase between 26°C and 65°C, rapid increase above 65°C
60 - 100
60°C: about 30% of maximal activity, 100°C: about 70% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
originally isolated from hot springs of the Yellowstone Park
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
optimal cell cultivation at pH 2.0 and 70°C
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). THPS_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
340
1
37262
Swiss-Prot
-
C4KFC9_SULIK
Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)
876
2
96662
TrEMBL
-
C3ND73_SULIY
Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)
554
2
61744
TrEMBL
-
C3NII3_SULIN
Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)
554
2
61758
TrEMBL
-
Q97WM0_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
443
6
48298
TrEMBL
-
A4YGR5_METS5
Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)
586
1
63893
TrEMBL
-
C3NAT5_SULIY
Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)
459
4
51891
TrEMBL
-
G4RN89_THETK
Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)
313
1
34446
TrEMBL
-
Q6KYY0_PICTO
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
493
2
55357
TrEMBL
-
C3ND84_SULIY
Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)
875
2
96530
TrEMBL
-
C4KEQ2_SULIK
Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)
452
4
50950
TrEMBL
-
C3N3G2_SULIA
Sulfolobus islandicus (strain M.16.27)
554
2
61700
TrEMBL
-
A4YFI4_METS5
Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)
952
1
102094
TrEMBL
-
G4RK32_THETK
Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)
1131
0
120053
TrEMBL
-
C3NK22_SULIN
Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)
459
4
51923
TrEMBL
-
C4KFD7_SULIK
Sulfolobus islandicus (strain M.16.4 / Kamchatka #3)
554
2
61769
TrEMBL
-
Q97WS9_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
570
2
63796
TrEMBL
-
C3NIH4_SULIN
Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)
875
2
96523
TrEMBL
-
Q97X65_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
556
2
61461
TrEMBL
-
Q6L2Q6_PICTO
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
739
1
82791
TrEMBL
-
C3MV67_SULIM
Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)
452
4
50829
TrEMBL
-
A4YG39_METS5
Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)
320
0
34705
TrEMBL
-
C3MNK4_SULIL
Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)
554
2
61855
TrEMBL
-
C3MNL2_SULIL
Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)
876
2
96758
TrEMBL
-
C3MVT5_SULIM
Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)
876
2
96672
TrEMBL
-
Q4J6X2_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
548
2
61464
TrEMBL
-
C3MNY0_SULIL
Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)
452
4
50959
TrEMBL
-
C3MVU3_SULIM
Sulfolobus islandicus (strain M.14.25 / Kamchatka #1)
554
2
61686
TrEMBL
-
C3N3F4_SULIA
Sulfolobus islandicus (strain M.16.27)
876
2
96676
TrEMBL
-
D0KP89_SACS9
Saccharolobus solfataricus (strain 98/2)
556
2
61461
TrEMBL
-
Q4J8N9_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
640
2
70280
TrEMBL
-
Q97WS1_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
875
0
96499
TrEMBL
-
Q97YX7_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
601
0
65103
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32651
32651
-
x * 32651, amino acid sequence calculation, x * 46000-51000, glycosylated enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 32651, amino acid sequence calculation, x * 46000-51000, glycosylated enzyme
monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
side-chain modification
glycoprotein
-
the enzyme has 11 potential glycosylation sites, e.g. at Asn24 and Asn28
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from cell culture by solubilization with detergents, ultrafiltration and five chromatographic steps to homogeneity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli inclusion bodies, expression in insect cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
overproduced in response to the peptide-enriched media
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli inclusion bodies by treatment with 8 M urea, incubation in acid solution, and gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fusek, M.; Lin, X.L.; Tang, J.
Enzymic properties of thermopsin
J. Biol. Chem.
265
1496-1501
1990
Sulfolobus acidocaldarius
brenda
Lin, X.L.; Tang, J.
Purification, characterization, and gene cloning of thermopsin, a thermostable acid protease from Sulfolobus acidocaldarius
J. Biol. Chem.
265
1490-1495
1990
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius (P17118)
brenda
Lin, X.; Tang, J.
Thermopsin
Methods Enzymol.
248
156-168
1995
Sulfolobus acidocaldarius
brenda
Lin, X.; Liu, M.; Tang, J.
Heterologous expression of thermopsin, a heat-stable acid proteinase
Enzyme Microb. Technol.
14
696-701
1992
Sulfolobus acidocaldarius
brenda
Lin, X.; Fusek, M.; Tang, J.
Thermopsin, a thermostable acid protease from Sulfolobus acidocaldarius
Adv. Exp. Med. Biol.
306
255-257
1991
Sulfolobus acidocaldarius
brenda
Tang, J.; Lin, X.
Thermopsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
225-227
2004
Sulfolobus acidocaldarius
-
brenda
Gogliettino, M.; Riccio, A.; Cocca, E.; Rossi, M.; Palmieri, G.; Balestrieri, M.
A new pepstatin-insensitive thermopsin-like protease overproduced in peptide-rich cultures of Sulfolobus solfataricus
Int. J. Mol. Sci.
15
3204-3219
2014
Saccharolobus solfataricus (Q97YX7), Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617 (Q97YX7)
brenda
Cannio, R.; Catara, G.; Fiume, I.; Balestrieri, M.; Rossi, M.; Palmieri, G.
Identification of a cell-bound extracellular protease overproduced by Sulfolobus solfataricus in peptide-rich media
Protein Pept. Lett.
17
78-85
2010
Saccharolobus solfataricus (Q97WS1), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97WS1)
brenda
Tsypysheva, I.; Petrova, P.; Kovalskaya, A.; Lobov, A.; Maksimova, M.; Zainullina, L.; Vinogradova, V.; Vakhitov, V.; Vakhitova, Y.; Galin, F.
Synthesis and cytotoxic activity of conjugates of (-)-cytisine and thermopsin amine derivatives with 1,3-dimethyl-5-formyluracil
Chem. Nat. Compd.
54
938-946
2018
Thermopsis schischkinii
-
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.4.23.42)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
