Aspartate-semialdehyde dehydrogenase: Difference between revisions

Latest revision as of 14:31, 20 March 2019

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]

3D Structures of Aspartate-semialdehyde dehydrogenase

Aspartate-semialdehyde dehydrogenase 3D structures

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

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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

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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 1: / Line 1: @@
-[[Image:1mc4.png|left|200px|thumb|Crystal Structure of Aspartate-semialdehyde dehydrogenase, [[1mc4]]]]
+<StructureSection load='1mb4' size='350' side='right' caption='Aspartate-semialdehyde dehydrogenase complex with NADP and substrate analog (PDB code [[1mb4]])' scene='45/452498/Cv/2'>
-{{STRUCTURE_1mc4|  PDB=1mc4  | SIZE=300| SCENE= |right|CAPTION=Aspartate-semialdehyde dehydrogenase, [[1mc4]] }}
+== 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 <scene name='45/452498/Cv/7'>active site</scene> and the <scene name='45/452498/Cv/9'>NADP-binding site</scene>.  The active site contains a <scene name='45/452498/Cv/10'>cysteine residue</scene> (C134 in ''Vibrio Cholerae'') which binds to inhibitors.  The C terminal contains the homodimer intersubunit contacts. <ref>PMID:12493825</ref>
+== 3D Structures of Aspartate-semialdehyde dehydrogenase ==
+[[Aspartate-semialdehyde dehydrogenase 3D structures]]
+</StructureSection>
+== References ==
+<references/>
+[[Category:Topic Page]]