Aspartate-semialdehyde dehydrogenase: Difference between revisions

Revision as of 17:38, 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 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)

Drag the structure with the mouse to rotate

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

Updated on 10-November-2015

ReferencesReferences

↑ 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

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

Alexander Berchansky, Michal Harel

[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

[1]

@@ Line 7: / Line 7: @@
 == 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 <scene name='45/452498/Cv/5'>cysteine residue</scene> (C134, in olive) 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 ''Vibrio Cholerae'') which binds to inhibitors.  The C terminal contains the homodimer intersubunit contacts. <ref>PMID:12493825</ref>
 </StructureSection>
@@ Line 58: / Line 58: @@
 **[[4r5m]] - VcASADH I + NADP + inhibitor<br />
 }}
+== References ==
+<references/>
 [[Category:Topic Page]]