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Aspartate-semialdehyde dehydrogenase: Difference between revisions

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{{STRUCTURE_1mc4|  PDB=1mc4  | SIZE=400| SCENE=Aspartate-semialdehyde_dehydrogenase/Cv/1 |right|CAPTION=Aspartate-semialdehyde dehydrogenase, [[1mc4]] }}
 
<StructureSection load='1mb4' size='340' side='right' caption='Tyrosine aminomutase complex with peptide-derived chromophore cofactor (PDB code [[2ohy]])' scene=''>
<StructureSection load='1mb4' size='340' side='right' caption='Aspartate-semialdehyde dehydrogenase complex with NADP and substrate analog (PDB code [[1mb4]])' scene=''>
 
== 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+.  
'''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 C terminal contains the homodimer intersubunit contacts.
</StructureSection>


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

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Alexander Berchansky, Michal Harel
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