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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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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Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WNX5 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WNX5 | - |
- |
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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L-aspartate 4-semialdehyde + phosphate + NADP+ | active site structure, overview | Mycobacterium tuberculosis | L-4-aspartyl phosphate + NADPH + H+ | - |
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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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L-aspartate 4-semialdehyde + phosphate + NADP+ | active site structure, overview | Mycobacterium tuberculosis H37Rv | L-4-aspartyl phosphate + NADPH + H+ | - |
r |
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 | Comment | Organism |
---|---|---|
ASADH | - |
Mycobacterium tuberculosis |
aspartyl beta-semialdehyde dehydrogenase | - |
Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | binding domain structure, overview | Mycobacterium tuberculosis |