BRENDA - Enzyme Database

Carboxymethylation of MutS-cysteine-15 specifically inactivates adenosylcobalamin-dependent glutamate mutase

Holloway, D.E.; Chen, H.P.; Marsh, E.N.G.; J. Biol. Chem. 271, 29121-29125 (1996)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
5.4.99.1
C15A
Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive
Clostridium tetanomorphum
5.4.99.1
C15N
Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive
Clostridium tetanomorphum
5.4.99.1
C15S
Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive
Clostridium tetanomorphum
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
5.4.99.1
iodoacetate
specifically alkylates Cys15 in enzyme component S with concomitant irreversible loss of enzyme activity
Clostridium tetanomorphum
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
5.4.99.1
Clostridium tetanomorphum
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.4.99.1
L-Glu
-
3459
Clostridium tetanomorphum
threo-3-Methylaspartate
-
3459
Clostridium tetanomorphum
-
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
5.4.99.1
Cobalamin
coenzyme binding and catalysis is very sensitive to mutations at position 15; dependent on
Clostridium tetanomorphum
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
5.4.99.1
Cobalamin
coenzyme binding and catalysis is very sensitive to mutations at position 15; dependent on
Clostridium tetanomorphum
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
5.4.99.1
C15A
Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive
Clostridium tetanomorphum
5.4.99.1
C15N
Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive
Clostridium tetanomorphum
5.4.99.1
C15S
Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive
Clostridium tetanomorphum
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
5.4.99.1
iodoacetate
specifically alkylates Cys15 in enzyme component S with concomitant irreversible loss of enzyme activity
Clostridium tetanomorphum
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.4.99.1
L-Glu
-
3459
Clostridium tetanomorphum
threo-3-Methylaspartate
-
3459
Clostridium tetanomorphum
-