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Literature summary extracted from

  • Tiffany, K.A.; Roberts, D.L.; Wang, M.; Paschke, R.; Mohsen, A.W.A.; Vockley, J.; Kim, J.J.P.
    Structure of human isovaleryl-CoA dehydrogenase at 2.6 ANG resolution: Structural basis for substrate specificity (1997), Biochemistry, 36, 8455-8464.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.8.4 initial crystallization performed by vapor diffusion using the hanging drop method following the sparse matrix protocol, final crystallization condition involves vapor diffusion using both hanging and sitting drop techniques, enzyme expressed in Escherichia coli crystallizes in the orthorhombic space group P212121 with unit cell parameters a: 94 A, b: 97.7 A, and c: 181.7 A Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.8.4 isovaleryl-CoA + acceptor Homo sapiens
-
3-methylcrotonyl-CoA + reduced acceptor
-
?
1.3.8.4 additional information Homo sapiens E254 of the enzyme is in close proximity to the bound FAD, E254 is the active site catalytic residue ?
-
?
1.3.8.4 additional information Homo sapiens the location of the catalytic residue together with a glycine at position 374 is important for conferring branched-chain substrate specificity to the enzyme ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.4 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.8.4 using DEAE-Sepharose followed by hydroxyapatite column chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.8.4 isovaleryl-CoA + acceptor
-
Homo sapiens 3-methylcrotonyl-CoA + reduced acceptor
-
?
1.3.8.4 additional information E254 of the enzyme is in close proximity to the bound FAD, E254 is the active site catalytic residue Homo sapiens ?
-
?
1.3.8.4 additional information the location of the catalytic residue together with a glycine at position 374 is important for conferring branched-chain substrate specificity to the enzyme Homo sapiens ?
-
?