BRENDA - Enzyme Database show

The catalytic machinery of a key enzyme in amino acid biosynthesis

Viola, R.E.; Faehnle, C.R.; Blanco, J.; Moore, R.A.; Liu, X.; Arachea, B.T.; Pavlovsky, A.G.; J. Amino Acids 2011, 352538 (2011)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
1.2.1.11
C136S
the mutation virtually eliminates catalysis
Haemophilus influenzae
1.2.1.11
E243D
the mutant shows 1.2% activity compared to the wild type enzyme
Haemophilus influenzae
1.2.1.11
H277N
the mutant shows 1% activity compared to the wild type enzyme
Haemophilus influenzae
1.2.1.11
K246R
the mutant shows 3.3% activity compared to the wild type enzyme
Haemophilus influenzae
1.2.1.11
R103K
the mutant shows 0.4% activity compared to the wild type enzyme
Haemophilus influenzae
1.2.1.11
R103L
the mutant shows 0.07% activity compared to the wild type enzyme
Haemophilus influenzae
1.2.1.11
R267L
the mutant shows 9.5% activity compared to the wild type enzyme
Haemophilus influenzae
1.2.1.11
R270K
the mutant shows 0.1% activity compared to the wild type enzyme
Haemophilus influenzae
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
Escherichia coli
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
Streptococcus pneumoniae
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
Candida albicans
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
Methanocaldococcus jannaschii
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
Haemophilus influenzae
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
Vibrio cholerae
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
r
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.11
Candida albicans
-
-
-
1.2.1.11
Escherichia coli
-
-
-
1.2.1.11
Haemophilus influenzae
P44801
-
-
1.2.1.11
Methanocaldococcus jannaschii
-
-
-
1.2.1.11
Streptococcus pneumoniae
-
-
-
1.2.1.11
Vibrio cholerae
Q9KQG2
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
-
725219
Escherichia coli
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
-
725219
Streptococcus pneumoniae
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
-
725219
Candida albicans
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
-
725219
Methanocaldococcus jannaschii
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
-
725219
Haemophilus influenzae
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
-
725219
Vibrio cholerae
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
725219
Escherichia coli
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
725219
Streptococcus pneumoniae
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
725219
Candida albicans
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
725219
Methanocaldococcus jannaschii
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
725219
Haemophilus influenzae
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
725219
Vibrio cholerae
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
Subunits
EC Number
Subunits
Commentary
Organism
1.2.1.11
homodimer
-
Candida albicans
1.2.1.11
homodimer
-
Escherichia coli
1.2.1.11
homodimer
-
Haemophilus influenzae
1.2.1.11
homodimer
-
Methanocaldococcus jannaschii
1.2.1.11
homodimer
-
Streptococcus pneumoniae
1.2.1.11
homodimer
-
Vibrio cholerae
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
-
Candida albicans
1.2.1.11
NADP+
-
Escherichia coli
1.2.1.11
NADP+
-
Haemophilus influenzae
1.2.1.11
NADP+
-
Methanocaldococcus jannaschii
1.2.1.11
NADP+
-
Streptococcus pneumoniae
1.2.1.11
NADP+
-
Vibrio cholerae
1.2.1.11
NADPH
-
Candida albicans
1.2.1.11
NADPH
-
Haemophilus influenzae
1.2.1.11
NADPH
-
Methanocaldococcus jannaschii
1.2.1.11
NADPH
-
Streptococcus pneumoniae
1.2.1.11
NADPH
-
Vibrio cholerae
1.2.1.11
NADPH
-
Escherichia coli
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
-
Candida albicans
1.2.1.11
NADP+
-
Escherichia coli
1.2.1.11
NADP+
-
Haemophilus influenzae
1.2.1.11
NADP+
-
Methanocaldococcus jannaschii
1.2.1.11
NADP+
-
Vibrio cholerae
1.2.1.11
NADP+
-
Streptococcus pneumoniae
1.2.1.11
NADPH
-
Candida albicans
1.2.1.11
NADPH
-
Escherichia coli
1.2.1.11
NADPH
-
Haemophilus influenzae
1.2.1.11
NADPH
-
Methanocaldococcus jannaschii
1.2.1.11
NADPH
-
Vibrio cholerae
1.2.1.11
NADPH
-
Streptococcus pneumoniae
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
1.2.1.11
C136S
the mutation virtually eliminates catalysis
Haemophilus influenzae
1.2.1.11
E243D
the mutant shows 1.2% activity compared to the wild type enzyme
Haemophilus influenzae
1.2.1.11
H277N
the mutant shows 1% activity compared to the wild type enzyme
Haemophilus influenzae
1.2.1.11
K246R
the mutant shows 3.3% activity compared to the wild type enzyme
Haemophilus influenzae
1.2.1.11
R103K
the mutant shows 0.4% activity compared to the wild type enzyme
Haemophilus influenzae
1.2.1.11
R103L
the mutant shows 0.07% activity compared to the wild type enzyme
Haemophilus influenzae
1.2.1.11
R267L
the mutant shows 9.5% activity compared to the wild type enzyme
Haemophilus influenzae
1.2.1.11
R270K
the mutant shows 0.1% activity compared to the wild type enzyme
Haemophilus influenzae
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
Escherichia coli
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
Streptococcus pneumoniae
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
Candida albicans
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
Methanocaldococcus jannaschii
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
Haemophilus influenzae
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
Vibrio cholerae
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
r
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
-
725219
Escherichia coli
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
-
725219
Streptococcus pneumoniae
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
-
725219
Candida albicans
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
-
725219
Methanocaldococcus jannaschii
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
-
725219
Haemophilus influenzae
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
1.2.1.11
L-4-aspartyl phosphate + NADPH + H+
-
725219
Vibrio cholerae
L-aspartate 4-semialdehyde + phosphate + NADP+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
725219
Escherichia coli
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
725219
Streptococcus pneumoniae
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
725219
Candida albicans
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
725219
Methanocaldococcus jannaschii
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
725219
Haemophilus influenzae
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
725219
Vibrio cholerae
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.2.1.11
homodimer
-
Candida albicans
1.2.1.11
homodimer
-
Escherichia coli
1.2.1.11
homodimer
-
Haemophilus influenzae
1.2.1.11
homodimer
-
Methanocaldococcus jannaschii
1.2.1.11
homodimer
-
Streptococcus pneumoniae
1.2.1.11
homodimer
-
Vibrio cholerae
General Information
EC Number
General Information
Commentary
Organism
1.2.1.11
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
Candida albicans
1.2.1.11
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
Escherichia coli
1.2.1.11
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
Haemophilus influenzae
1.2.1.11
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
Methanocaldococcus jannaschii
1.2.1.11
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
Streptococcus pneumoniae
1.2.1.11
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
Vibrio cholerae
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.2.1.11
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
Candida albicans
1.2.1.11
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
Escherichia coli
1.2.1.11
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
Haemophilus influenzae
1.2.1.11
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
Methanocaldococcus jannaschii
1.2.1.11
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
Streptococcus pneumoniae
1.2.1.11
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
Vibrio cholerae