3.4.21.65: Thermomycolin
This is an abbreviated version!
For detailed information about Thermomycolin, go to the full flat file.
Word Map on EC 3.4.21.65
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3.4.21.65
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3.4.21.14
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subtilisins
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carlsberg
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alpha-chymotrypsin
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tritirachium
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voordouw
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limber
- 3.4.21.65
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3.4.21.14
- subtilisins
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carlsberg
- alpha-chymotrypsin
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tritirachium
-
voordouw
-
limber
Reaction
Rather nonspecific hydrolysis of proteins. Preferential cleavage: Ala-/-, Tyr-/-, Phe-/- in small molecule substrates =
Synonyms
EC 3.4.21.14, EC 3.4.4.16, Proteinase, Malbranchea pulchella sulfurea extracellular, Thermomycolase
ECTree
3.4.21.65 ThermomycolinAdvanced search results
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Substrates Products on EC 3.4.21.65 - Thermomycolin
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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
Glucagon + H2O
Hydrolyzed glucagon
-
preferential cleavage of Thr5-Phe6, Ser8-Asp9, Lys12-Tyr13, Asp15-Ser16, Ser16-Arg17 and Arg17-Arg18, no amino acids observed in the digest
no amino acids observed in the digest
?
Oxidized insulin A-chain + H2O
Hydrolyzed oxidized insulin A-chain
-
-
-
-
?
Oxidized insulin A-chain + H2O
Hydrolyzed oxidized insulin A-chain
-
no amino acids observed in the digest
no amino acids observed in the digest
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
-
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
no amino acids observed in the digest
no amino acids observed in the digest
?
additional information
?
-
-
slow release of peptides from native collagen
-
-
?
additional information
?
-
-
slow release of peptides from native collagen
-
-
?
additional information
?
-
-
active site sequence: Leu-Ser-(Gly)-Thr-Ser-Met
-
-
?
additional information
?
-
-
specificity towards small synthetic ester substrates: preference in decreasing order for L-Ala, L-Tyr, L-Phe, Gly, L-Leu, L-Trp, L-Val, L-Lys, L-Pro on the carboxyl side of the bond hydrolyzed
-
-
?
additional information
?
-
-
no well-defined specificity for particular amino acid residues is evident, but ready hydrolysis of peptide bonds within sequences containing non-polar residues
-
-
?
additional information
?
-
-
small synthetic ester substrates are preferentially hydrolyzed at bonds situated on the carboxyl side of aromatic or apolar amino acid residues which are not beta-branched, positively charged or of the D-configuration
-
-
?
