Aspartate-semialdehyde dehydrogenase: Difference between revisions

Revision as of 17:36, 10 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 and the . The active site contains a (C134, in olive) 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 10-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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 == Structural highlights ==
-ASADH contains 2 domains.  The N terminal domain contains the <scene name='45/452498/Cv/3'>active site</scene> and the <scene name='45/452498/Cv/4'>NADP-binding site</scene>.  The active site contains a cysteine residue which binds to inhibitors.  The C terminal contains the homodimer intersubunit contacts.
+ASADH contains 2 domains.  The N terminal domain contains the <scene name='45/452498/Cv/3'>active site</scene> and the <scene name='45/452498/Cv/4'>NADP-binding site</scene>.  The active site contains a <scene name='45/452498/Cv/5'>cysteine residue</scene> (C134, in olive) which binds to inhibitors.  The C terminal contains the homodimer intersubunit contacts.
 </StructureSection>