Aspartate-semialdehyde dehydrogenase: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
Michal Harel (talk | contribs)
No edit summary
No edit summary
Line 1: Line 1:
<StructureSection load='1mb4' size='340' side='right' caption='Aspartate-semialdehyde dehydrogenase complex with NADP and substrate analog (PDB code [[1mb4]])' scene=''>
<StructureSection load='1mb4' size='450' side='right' caption='Aspartate-semialdehyde dehydrogenase complex with NADP and substrate analog (PDB code [[1mb4]])' scene='45/452498/Cv/2'>


== Function ==
== Function ==

Revision as of 17:19, 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 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)

Drag the structure with the mouse to rotate

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