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Activity and spectroscopic properties of the Escherichia coli glutamate 1-semialdehyde aminotransferase and the putative active site mutant K265R

Ilag, L.L.; Jahn, D.; Biochemistry 31, 7143-7151 (1992)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
5.4.3.8
ethanolamine
stimulates activity of mutant enzyme Lys265Arg
Escherichia coli
5.4.3.8
methylamine
stimulates activity of mutant enzyme Lys265Arg
Escherichia coli
Cloned(Commentary)
EC Number
Commentary
Organism
5.4.3.8
mutant enzyme Lys265Arg, overexpression
Escherichia coli
Engineering
EC Number
Amino acid exchange
Commentary
Organism
5.4.3.8
L265E
mutant Lys265Arg has 2% of the enzymatic activity compared to the wild-type enzyme, the dimeric structure is not influenced, activity is stimulated by addition of exogenous amines such as ethanolamine and methylamine
Escherichia coli
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5.4.3.8
(S)-4-Amino-5-oxopentanoate
Escherichia coli
4,5-dioxovalerate and 4,5-diaminovalerate are reaction intermediates
?
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
5.4.3.8
Escherichia coli
-
wild-type and active site mutant K265R
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.4.3.8
(S)-4-Amino-5-oxopentanoate
-
3432
Escherichia coli
5-Amino-4-oxopentanoate
-
3432
Escherichia coli
-
5.4.3.8
(S)-4-Amino-5-oxopentanoate
4,5-dioxovalerate and 4,5-diaminovalerate are reaction intermediates
3432
Escherichia coli
?
-
-
-
-
5.4.3.8
4,5-Diaminovalerate
is a substrate for the pyridoxal 5'-phosphate form of the enzyme
3432
Escherichia coli
?
-
-
-
-
5.4.3.8
4,5-Dioxovalerate
is a substrate for the pyridoxamine form of the enzyme
3432
Escherichia coli
5-Amino-4-oxopentanoate
-
3432
Escherichia coli
-
Subunits
EC Number
Subunits
Commentary
Organism
5.4.3.8
dimer
-
Escherichia coli
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
5.4.3.8
ethanolamine
stimulates activity of mutant enzyme Lys265Arg
Escherichia coli
5.4.3.8
methylamine
stimulates activity of mutant enzyme Lys265Arg
Escherichia coli
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
5.4.3.8
mutant enzyme Lys265Arg, overexpression
Escherichia coli
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
5.4.3.8
L265E
mutant Lys265Arg has 2% of the enzymatic activity compared to the wild-type enzyme, the dimeric structure is not influenced, activity is stimulated by addition of exogenous amines such as ethanolamine and methylamine
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5.4.3.8
(S)-4-Amino-5-oxopentanoate
Escherichia coli
4,5-dioxovalerate and 4,5-diaminovalerate are reaction intermediates
?
-
-
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.4.3.8
(S)-4-Amino-5-oxopentanoate
-
3432
Escherichia coli
5-Amino-4-oxopentanoate
-
3432
Escherichia coli
-
5.4.3.8
(S)-4-Amino-5-oxopentanoate
4,5-dioxovalerate and 4,5-diaminovalerate are reaction intermediates
3432
Escherichia coli
?
-
-
-
-
5.4.3.8
4,5-Diaminovalerate
is a substrate for the pyridoxal 5'-phosphate form of the enzyme
3432
Escherichia coli
?
-
-
-
-
5.4.3.8
4,5-Dioxovalerate
is a substrate for the pyridoxamine form of the enzyme
3432
Escherichia coli
5-Amino-4-oxopentanoate
-
3432
Escherichia coli
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
5.4.3.8
dimer
-
Escherichia coli