Aspartate-semialdehyde dehydrogenase
From Proteopedia
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(New page: Crystal Structure of Aspartate-semialdehyde dehydrogenase, 1mc4 {{STRUCTURE_1mc4| PDB=1mc4 | SIZE=300| SCENE= |right|CAPTION=Aspartate-semialdehyd...) |
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| - | + | <StructureSection load='1mb4' size='350' side='right' caption='Aspartate-semialdehyde dehydrogenase complex with NADP and substrate analog (PDB code [[1mb4]])' scene='45/452498/Cv/2'> | |
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| + | == Function == | ||
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| + | '''Aspartate-semialdehyde dehydrogenase''' (ASADH) is an enzyme which is part of the biosynthesis of amino acids in bacteria, plants and fungi. It catalyzes the conversion of L-aspartate 4-semialdehyde (ASA) + phosphate + NADP to L-4-aspartyl phosphate + NADPH + H+. | ||
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| + | == Structural highlights == | ||
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| + | ASADH contains 2 domains. The N terminal domain contains the <scene name='45/452498/Cv/7'>active site</scene> and the <scene name='45/452498/Cv/9'>NADP-binding site</scene>. The active site contains a <scene name='45/452498/Cv/10'>cysteine residue</scene> (C134 in ''Vibrio Cholerae'') which binds to inhibitors. The C terminal contains the homodimer intersubunit contacts. <ref>PMID:12493825</ref> | ||
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| + | == 3D Structures of Aspartate-semialdehyde dehydrogenase == | ||
| + | [[Aspartate-semialdehyde dehydrogenase 3D structures]] | ||
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| + | </StructureSection> | ||
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| + | == References == | ||
| + | <references/> | ||
| + | [[Category:Topic Page]] | ||
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