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Literature summary extracted from

  • Begley, D.W.; Davies, D.R.; Hartley, R.C.; Hewitt, S.N.; Rychel, A.L.; Myler, P.J.; Van Voorhis, W.C.; Staker, B.L.; Stewart, L.J.
    Probing conformational states of glutaryl-CoA dehydrogenase by fragment screening (2011), Acta Crystallogr. Sect. F, 67, 1060-1069.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.8.6 DNA and amino acid sequence determination annd analysis, phylogenetic tree, expression with a cleavable 6-His fusion tag followed by the human rhinovirus 3C protease-cleavage sequence in Escherichia coli strain BL21 (DE3) Burkholderia pseudomallei

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.8.6 purified detagged recombinant apoenzyme without FAD, sitting drop vapor diffusion method, 26 mg/ml protein in 25 mM Tris pH 8.0, 200 mM NaCl, 1% glycerol, and 1 mM TCEP, with reservoir solution consisting of 20% PEG 3000, 100 mM HEPES, 200 mM NaCl, pH 7.5, 16°C, X-ray diffraction structure determination and analysis at 1.99-2.40 A resolution Burkholderia pseudomallei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.8.6 glutaryl-CoA + electron transfer flavoprotein Homo sapiens
-
 (E)-but-2-enoyl-CoA + CO2 + reduced electron transfer flavoprotein
-
 ?
1.3.8.6 glutaryl-CoA + electron transfer flavoprotein Burkholderia pseudomallei
-
 (E)-but-2-enoyl-CoA + CO2 + reduced electron transfer flavoprotein
-
 ?
1.3.8.6 glutaryl-CoA + electron transfer flavoprotein Burkholderia pseudomallei 1710b
-
 (E)-but-2-enoyl-CoA + CO2 + reduced electron transfer flavoprotein
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.6 Burkholderia pseudomallei Q3JP94
-
-
1.3.8.6 Burkholderia pseudomallei 1710b Q3JP94
-
-
1.3.8.6 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.8.6 recombinant His6-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration Burkholderia pseudomallei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.8.6 glutaryl-CoA + electron transfer flavoprotein
-
 Homo sapiens (E)-but-2-enoyl-CoA + CO2 + reduced electron transfer flavoprotein
-
 ?
1.3.8.6 glutaryl-CoA + electron transfer flavoprotein
-
 Burkholderia pseudomallei (E)-but-2-enoyl-CoA + CO2 + reduced electron transfer flavoprotein
-
 ?
1.3.8.6 glutaryl-CoA + electron transfer flavoprotein
-
 Burkholderia pseudomallei 1710b (E)-but-2-enoyl-CoA + CO2 + reduced electron transfer flavoprotein
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.8.6 GCDH
-
 Homo sapiens
1.3.8.6 GCDH
-
 Burkholderia pseudomallei

General Information

EC Number General Information Comment Organism
1.3.8.6 evolution glutaryl-CoA dehydrogenase belongs to the acyl-CoA dehydrogenase enzyme family Homo sapiens
1.3.8.6 evolution glutaryl-CoA dehydrogenase belongs to the acyl-CoA dehydrogenase enzyme family, phylogenetic tree, overview Burkholderia pseudomallei
1.3.8.6 malfunction defects in glutaryl-CoA dehydrogenase are involved in glutaric acidemia type 1, an inherited metabolic disorder which can cause macrocephaly, muscular rigidity, spastic paralysis and other progressive movement disorders in humans Homo sapiens
1.3.8.6 metabolism the enzyme catalyzes an intermediate step in the metabolic breakdown of lysine and tryptophan Homo sapiens
1.3.8.6 metabolism the enzyme catalyzes an intermediate step in the metabolic breakdown of lysine and tryptophan Burkholderia pseudomallei
1.3.8.6 additional information the apo structure of GCDH from Burkholderia pseudomallei reveals a loss of secondary structure and increased disorder in the cofactor-binding pocket relative to the ternary complex of the highly homologous human GCDH Burkholderia pseudomallei