Information on EC 3.4.21.65 - Thermomycolin

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The expected taxonomic range for this enzyme is: Malbranchea pulchella

EC NUMBER
COMMENTARY hide
3.4.21.65
-
RECOMMENDED NAME
GeneOntology No.
Thermomycolin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Rather nonspecific hydrolysis of proteins. Preferential cleavage: Ala-/-, Tyr-/-, Phe-/- in small molecule substrates
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
52233-31-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Acetyl-Ala-Ala-Ala methyl ester + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O
?
show the reaction diagram
-
-
-
-
-
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
show the reaction diagram
-
-
-
-
-
Carboxybenzoyl-Gly 4-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
-
Carboxybenzoyl-L-Ala 4-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
-
Carboxybenzoyl-L-Phe 4-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
-
casein + H2O
hydrolyzed casein
show the reaction diagram
-
-
-
-
-
Elastin-Congo Red + H2O
Hydrolyzed elastin-Congo Red
show the reaction diagram
-
-
-
-
-
Glucagon + H2O
Hydrolyzed glucagon
show the reaction diagram
Oxidized insulin A-chain + H2O
Hydrolyzed oxidized insulin A-chain
show the reaction diagram
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-Methylphenylsulfonyl fluorides
-
-
4-Nitrophenylsulfonyl fluorides
-
-
Carboxybenzoyl halomethyl ketones
-
L-Phe-CH2Cl and L-Phe-CH2Br
-
Egg white trypsin inhibitor
-
-
-
Lima bean trypsin inhibitor
-
-
-
Phenylmethylsulfonyl fluorides
-
-
-
Serine protease inhibitors
-
-
-
Soybean trypsin inhibitor
-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
Acetyl-Ala-Ala-Ala methyl ester
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2050
Acetyl-Ala-Ala-Ala methyl ester
Malbranchea pulchella
-
-
additional information
additional information
Malbranchea pulchella
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11000 - 17500
-
Malbranchea pulchella var. sulfurea, gel filtration
32000 - 33000
-
Malbranchea pulchella, sedimentation equilibrium, of diisopropylphosphorylthermomycolase
32000
-
Malbranchea pulchella var. sulfurea, sedimentation equilibrium measurement
32700
-
Malbranchea pulchella var. sulfurea, amino acid analysis
33000
-
x * 33000, Malbranchea pulchella var. sulfurea, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
-
rapid and irreversible denaturation below
29526
4.5 - 10.5
-
30C, 2 h, stable
29526, 29531
6 - 9.6
-
30C, 20 h, stable
29526, 29531
6.5 - 9.5
-
30C, 20 h, stable
29531
8.5
-
optimum pH for stability
29526, 29531
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
maximal thermostability 10 mM Ca2+
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Autolysis, which is the dominant inactivation process below 50C, is decreased by the presence of calcium or macromolecules
-
Calcium stabilizes against autolysis
-
Denaturation by freeze-drying
-
Denaturation by freezing
-
Extensive autolysis, especially at low calcium concentrations produces low MW peptide material
-
Freezing and freeze-drying causes a considerable loss of activity
-
Macromolecules and Ca2+ provide protection against significant autolysis
-
No loss of activity after 12 h of agitation on a reciprocal shaker in the absence of silicone antifoam agent or in the presence of both the antifoam agent and 5% Ficoll
-
Particularly thermostable in the presence of Ca2+
-
Repeated freeze-drying causes insolubilization
-
Urea denaturation, 8 M, is markedly inhibited by the binding of a single Ca2+
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE