Aspartate-semialdehyde dehydrogenase: Difference between revisions

Revision as of 14:48, 5 November 2015

Function

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+.

Structural highlights

ASADH contains 2 domains. The N terminal domain contains the active site and the NADP-binding site. The active site contains a cysteine residue which binds to inhibitors. The C terminal contains the homodimer intersubunit contacts.

Aspartate-semialdehyde dehydrogenase complex with NADP and substrate analog (PDB code 1mb4)

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3D Structures of Aspartate-semialdehyde dehydrogenase3D Structures of Aspartate-semialdehyde dehydrogenase

Updated on 05-November-2015

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel

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 <StructureSection load='1mb4' size='340' side='right' caption='Aspartate-semialdehyde dehydrogenase complex with NADP and substrate analog (PDB code [[1mb4]])' scene=''>
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 == Structural highlights ==
-ASADH contains 2 domains.  The N terminal domain contains the active site and the NADP-binding site.  The C terminal contains the homodimer intersubunit contacts.
+ASADH contains 2 domains.  The N terminal domain contains the active site and the NADP-binding site.  The active site contains a cysteine residue which binds to inhibitors.  The C terminal contains the homodimer intersubunit contacts.
 </StructureSection>