Aspartate-semialdehyde dehydrogenase: Difference between revisions

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**[[5cef]] – ASADH – ''Cryptococcus neoformans''<br />
**[[5cef]] – ASADH – ''Cryptococcus neoformans''<br />
**[[5jw6]] – ASADH – ''Neosartorya fumigata''<br />
**[[5jw6]] – ASADH – ''Neosartorya fumigata''<br />
**[[6bac]] - ASADH – ''Neisseria gonorrhoeae''<br />


*ASADH binary complex
*ASADH binary complex

Revision as of 13:44, 22 March 2018


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 Vibrio Cholerae) which binds to inhibitors. The C terminal contains the homodimer intersubunit contacts. [1]


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 22-March-2018

ReferencesReferences

  1. ↑ Blanco J, Moore RA, Kabaleeswaran V, Viola RE. A structural basis for the mechanism of aspartate-beta-semialdehyde dehydrogenase from Vibrio cholerae. Protein Sci. 2003 Jan;12(1):27-33. PMID:12493825

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Alexander Berchansky, Michal Harel
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