1.3.99.32: glutaryl-CoA dehydrogenase (acceptor)
This is an abbreviated version!
For detailed information about glutaryl-CoA dehydrogenase (acceptor), go to the full flat file.
Word Map on EC 1.3.99.32
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1.3.99.32
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dehydratase
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myopathies
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co2
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monounsaturated
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3-hydroxyacyl-coa
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crotonyl-coa
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glutaconyl-coa
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geobacter
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metallireducens
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vlcfas
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dehydrogenate
- 1.3.99.32
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dehydratase
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myopathies
- co2
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monounsaturated
- 3-hydroxyacyl-coa
- crotonyl-coa
- glutaconyl-coa
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geobacter
- metallireducens
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vlcfas
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dehydrogenate
Reaction
Synonyms
GDH, GDHDes, glutaryl-CoA dehydrogenase (non-decarboxylating), glutaryl-coenzyme A dehydrogenase, nondecarboxylating glutaryl-coenzyme A dehydrogenase, nondecarboxylating, glutaconyl-coenzyme A-forming GDH
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Natural Substrates Products
Natural Substrates Products on EC 1.3.99.32 - glutaryl-CoA dehydrogenase (acceptor)
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REACTION DIAGRAM
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GDHGeo contains highly conserved amino acid residues that are specifically involved in the decarboxylation of the intermediate glutaconyl-CoA
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additional information
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GDHGeo contains highly conserved amino acid residues that are specifically involved in the decarboxylation of the intermediate glutaconyl-CoA
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additional information
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the decarboxylating, EC 1.3.99.7, and nondecarboxylating capabilities are provided by complex structural changes around the glutaconyl carboxylate group, the key factor being a Tyr to Val exchange strictly conserved between the two GDH types, the interaction between the glutaconyl carboxylate and the guanidinium group of a conserved Arg is stronger in GDHDes than in the decarboxylating enzyme, molecular dynamics. The identified structural changes prevent decarboxylation 1. by strengthening the C4-C5 bond of glutaconyl-CoA, 2. by reducing the leaving group potential of CO2, and 3. by increasing the distance between the C4 atom, negatively charged in the dienolate transition state, and the adjacent glutamic acid
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