Aspartate-semialdehyde dehydrogenase
From Proteopedia
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- | <StructureSection load='1mb4' size='340' side='right' caption=' | + | <StructureSection load='1mb4' size='340' side='right' caption='Aspartate-semialdehyde dehydrogenase complex with NADP and substrate analog (PDB code [[1mb4]])' scene=''> |
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+ | == Function == | ||
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'''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+. | ||
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+ | == Structural highlights == | ||
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+ | 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. | ||
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+ | </StructureSection> | ||
== 3D Structures of Aspartate-semialdehyde dehydrogenase == | == 3D Structures of Aspartate-semialdehyde dehydrogenase == |
Revision as of 11:36, 5 November 2015
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3D Structures of Aspartate-semialdehyde dehydrogenase
Updated on 05-November-2015