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show all sequences of 6.3.3.4

Kinetic mechanism of the beta-Lactam synthetase of Streptomyces clavuligerus

Bachmann, B.O.; Townsend, C.A.; Biochemistry 39, 11187-11193 (2000)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
deoxyamidinoproclavaminate
product inhibition
Streptomyces clavuligerus
diphosphate
product inhibition
Streptomyces clavuligerus
N2-(carboxymethyl)-L-arginine
competitive to N2-(carboxyethyl)-L-arginine
Streptomyces clavuligerus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.153
-
ATP
pH 7.5
Streptomyces clavuligerus
0.22
-
N2-(carboxyethyl)-L-arginine
pH 7.5
Streptomyces clavuligerus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N2-(carboxyethyl)-L-arginine + ATP
Streptomyces clavuligerus
early step in clavulanic acid biosynthesis
AMP + diphosphate + deoxyamidinoproclavaminate
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces clavuligerus
P0DJQ7
-
-
Purification (Commentary)
Commentary
Organism
recombinant protein expressed in E. coli
Streptomyces clavuligerus
Reaction
Reaction
Commentary
Organism
ATP + L-N2-(2-carboxyethyl)arginine = AMP + diphosphate + deoxyamidinoproclavaminate
it has been proposed that L-N2-(2-carboxyethyl)arginine is first converted into an acyl-AMP by reaction with ATP and loss of diphosphate, and that the beta-lactam ring is then formed by the intramolecular attack of the beta-nitrogen on the activated carboxy group, in a sequential ordered bi-ter kinetic mechanism
Streptomyces clavuligerus
Storage Stability
Storage Stability
Organism
-20°C, 50 mM Tris-HCl, 10% glycerol, 2 mM dithiothreitol, 0.01 mM EDTA, pH 7.5, stable
Streptomyces clavuligerus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N2-(carboxyethyl)-L-arginine + ATP
mechanism
639032
Streptomyces clavuligerus
AMP + diphosphate + deoxyamidinoproclavaminate
-
-
-
?
N2-(carboxyethyl)-L-arginine + ATP
early step in clavulanic acid biosynthesis
639032
Streptomyces clavuligerus
AMP + diphosphate + deoxyamidinoproclavaminate
-
-
-
-
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
deoxyamidinoproclavaminate
product inhibition
Streptomyces clavuligerus
diphosphate
product inhibition
Streptomyces clavuligerus
N2-(carboxymethyl)-L-arginine
competitive to N2-(carboxyethyl)-L-arginine
Streptomyces clavuligerus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.153
-
ATP
pH 7.5
Streptomyces clavuligerus
0.22
-
N2-(carboxyethyl)-L-arginine
pH 7.5
Streptomyces clavuligerus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N2-(carboxyethyl)-L-arginine + ATP
Streptomyces clavuligerus
early step in clavulanic acid biosynthesis
AMP + diphosphate + deoxyamidinoproclavaminate
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant protein expressed in E. coli
Streptomyces clavuligerus
Storage Stability (protein specific)
Storage Stability
Organism
-20°C, 50 mM Tris-HCl, 10% glycerol, 2 mM dithiothreitol, 0.01 mM EDTA, pH 7.5, stable
Streptomyces clavuligerus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N2-(carboxyethyl)-L-arginine + ATP
mechanism
639032
Streptomyces clavuligerus
AMP + diphosphate + deoxyamidinoproclavaminate
-
-
-
?
N2-(carboxyethyl)-L-arginine + ATP
early step in clavulanic acid biosynthesis
639032
Streptomyces clavuligerus
AMP + diphosphate + deoxyamidinoproclavaminate
-
-
-
-
Other publictions for EC 6.3.3.4
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
742159
Shrestha
-
Heterologous production of cl ...
Streptomyces clavuligerus, Streptomyces clavuligerus DSM 738
Biotechnol. Bioprocess Eng.
22
359-365
2017
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728238
Labonte
Engineering the synthetic pote ...
Streptomyces clavuligerus
MedChemComm
3
960-966
2012
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3
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13
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1
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1
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5
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13
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1
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1
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3
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13
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1
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5
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13
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639033
Miller
The catalytic cycle of beta-la ...
Streptomyces clavuligerus
Proc. Natl. Acad. Sci. USA
99
14752-14757
2002
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1
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1
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1
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639036
Townsend
New reactions in clavulanic ac ...
Streptomyces clavuligerus
Curr. Opin. Chem. Biol.
6
583-589
2002
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639034
Miller
Structure of beta-lactam synth ...
Streptomyces clavuligerus
Nat. Struct. Biol.
8
684-689
2001
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639032
Bachmann
Kinetic mechanism of the beta- ...
Streptomyces clavuligerus
Biochemistry
39
11187-11193
2000
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2
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639031
Bachmann
beta-Lactam synthetase: a new ...
Streptomyces clavuligerus
Proc. Natl. Acad. Sci. USA
95
9082-9086
1998
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1
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639035
McNaughton
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beta-Lactam synthetase: implic ...
Streptomyces clavuligerus
Chem. Commun. (Camb.)
1998
2325-2326
1998
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