KEGG   ENZYME: 1.3.99.32Help
Entry
EC 1.3.99.32                Enzyme                                 

Name
glutaryl-CoA dehydrogenase (acceptor);
GDHDes;
nondecarboxylating glutaryl-coenzyme A dehydrogenase;
nondecarboxylating glutaconyl-coenzyme A-forming GDH;
glutaryl-CoA dehydrogenase (non-decarboxylating)
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With other, unknown, acceptors
BRITE hierarchy
Sysname
glutaryl-CoA:acceptor 2,3-oxidoreductase (non-decarboxylating)
Reaction(IUBMB)
glutaryl-CoA + acceptor = (E)-glutaconyl-CoA + reduced acceptor [RN:R05579]
Reaction(KEGG)
Substrate
glutaryl-CoA [CPD:C00527];
acceptor [CPD:C00028]
Product
(E)-glutaconyl-CoA [CPD:C02411];
reduced acceptor [CPD:C00030]
Comment
The enzyme contains FAD. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (EC 1.3.8.6), and a nondecarboxylating enzyme (this entry). The two enzymes cause different structural changes around the glutaconyl carboxylate group, primarily due to the presence of either a tyrosine or a valine residue, respectively, at the active site.
History
EC 1.3.99.32 created 2012, modified 2013
Pathway
Benzoate degradation
Microbial metabolism in diverse environments
Orthology
K16173  
glutaryl-CoA dehydrogenase (non-decarboxylating)
Genes
GBM: 
GEO: 
GEM: 
DAL: 
DAT: 
HRM2_38550(acd11) HRM2_38670(acd12)
SAT: 
DTI: 
DBR: 
BAG: 
GTH: 
GWC: 
GMC: 
AFL: 
Aflv_1240(acdA)
DKU: 
DOR: 
DAI: 
CHY: 
 » show all
Taxonomy
Reference
1  [PMID:19395484]
  Authors
Wischgoll S, Taubert M, Peters F, Jehmlich N, von Bergen M, Boll M
  Title
Decarboxylating and nondecarboxylating glutaryl-coenzyme A dehydrogenases in the  aromatic metabolism of obligately anaerobic bacteria.
  Journal
J. Bacteriol. 191 (2009) 4401-9.
  Sequence
[up:C3UVB0]
Reference
2  [PMID:20486657]
  Authors
Wischgoll S, Demmer U, Warkentin E, Gunther R, Boll M, Ermler U
  Title
Structural basis for promoting and preventing decarboxylation in glutaryl-coenzyme a dehydrogenases.
  Journal
Biochemistry. 49 (2010) 5350-7.
  Sequence
[up:C3UVB0]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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