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Molecular modelling and comparative structural account of aspartyl beta-semialdehyde dehydrogenase of Mycobacterium tuberculosis (H37Rv)

Singh, A.; Kushwaha, H.R.; Sharma, P.; J. Mol. Model. 14, 249-263 (2008)

Data extracted from this reference:

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-aspartate 4-semialdehyde + phosphate + NADP+
Mycobacterium tuberculosis
ASADH is an important enzyme, occupying the first branch position of the biosynthetic pathway of the aspartate family of amino acids, i.e. lysine, methionine, isoleucine and threonine, L-aspartate-beta-semialdehyde is a key intermediate in the biosynthesis of diaminopimelic acid
L-4-aspartyl phosphate + NADPH + H+
-
-
r
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.11
Mycobacterium tuberculosis
P9WNX5
-
-
1.2.1.11
Mycobacterium tuberculosis H37Rv
P9WNX5
-
-
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-aspartate 4-semialdehyde + phosphate + NADP+
ASADH is an important enzyme, occupying the first branch position of the biosynthetic pathway of the aspartate family of amino acids, i.e. lysine, methionine, isoleucine and threonine, L-aspartate-beta-semialdehyde is a key intermediate in the biosynthesis of diaminopimelic acid
688468
Mycobacterium tuberculosis
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
active site structure, overview
688468
Mycobacterium tuberculosis
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
Subunits
EC Number
Subunits
Commentary
Organism
1.2.1.11
dimer
dimerization domain structure, overview
Mycobacterium tuberculosis
1.2.1.11
More
secondary structure topology, homology modelling and enzyme structure analysis, comparison of the three-dimensional fold and comparative modelling, overview, the fist alphabeta unit contains the highly conserved GxxGxxG NAD-binding motif
Mycobacterium tuberculosis
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
binding domain structure, overview
Mycobacterium tuberculosis
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
binding domain structure, overview
Mycobacterium tuberculosis
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-aspartate 4-semialdehyde + phosphate + NADP+
Mycobacterium tuberculosis
ASADH is an important enzyme, occupying the first branch position of the biosynthetic pathway of the aspartate family of amino acids, i.e. lysine, methionine, isoleucine and threonine, L-aspartate-beta-semialdehyde is a key intermediate in the biosynthesis of diaminopimelic acid
L-4-aspartyl phosphate + NADPH + H+
-
-
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-aspartate 4-semialdehyde + phosphate + NADP+
ASADH is an important enzyme, occupying the first branch position of the biosynthetic pathway of the aspartate family of amino acids, i.e. lysine, methionine, isoleucine and threonine, L-aspartate-beta-semialdehyde is a key intermediate in the biosynthesis of diaminopimelic acid
688468
Mycobacterium tuberculosis
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
active site structure, overview
688468
Mycobacterium tuberculosis
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.2.1.11
dimer
dimerization domain structure, overview
Mycobacterium tuberculosis
1.2.1.11
More
secondary structure topology, homology modelling and enzyme structure analysis, comparison of the three-dimensional fold and comparative modelling, overview, the fist alphabeta unit contains the highly conserved GxxGxxG NAD-binding motif
Mycobacterium tuberculosis