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Literature summary for 1.2.1.11 extracted from

  • Singh, A.; Kushwaha, H.R.; Sharma, P.
    Molecular modelling and comparative structural account of aspartyl beta-semialdehyde dehydrogenase of Mycobacterium tuberculosis (H37Rv) (2008), J. Mol. Model., 14, 249-263.
    View publication on PubMed
Search for more literature for 1.2.1.11

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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+
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 r
L-aspartate 4-semialdehyde + phosphate + NADP+ Mycobacterium tuberculosis H37Rv 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+
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 r

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WNX5
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Mycobacterium tuberculosis H37Rv P9WNX5
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Mycobacterium tuberculosis L-4-aspartyl phosphate + NADPH + H+
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 r
L-aspartate 4-semialdehyde + phosphate + NADP+ active site structure, overview Mycobacterium tuberculosis L-4-aspartyl phosphate + NADPH + H+
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 r
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 Mycobacterium tuberculosis H37Rv L-4-aspartyl phosphate + NADPH + H+
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 r
L-aspartate 4-semialdehyde + phosphate + NADP+ active site structure, overview Mycobacterium tuberculosis H37Rv L-4-aspartyl phosphate + NADPH + H+
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 r

Subunits

Subunits Comment Organism
dimer dimerization domain structure, overview Mycobacterium tuberculosis
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

Synonyms

Synonyms Comment Organism
ASADH
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 Mycobacterium tuberculosis
aspartyl beta-semialdehyde dehydrogenase
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 Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NADP+ binding domain structure, overview Mycobacterium tuberculosis