DB code: T00009

CATH domain 1.10.540.10 : Butyryl-Coa Dehydrogenase, subunit A; domain 1
2.40.110.10 : Butyryl-CoA Dehydrogenase, subunit A; domain 2
1.20.140.10 : Butyryl-CoA Dehydrogenase, subunit A; domain 3 Catalytic domain
E.C. 1.3.8.4
CSA 1ivh
M-CSA 1ivh
MACiE M0068

CATH domain Related DB codes (homologues)
1.10.540.10 : Butyryl-Coa Dehydrogenase, subunit A; domain 1 T00007 T00008
1.20.140.10 : Butyryl-CoA Dehydrogenase, subunit A; domain 3 T00007 T00008
2.40.110.10 : Butyryl-CoA Dehydrogenase, subunit A; domain 2 T00007 T00008

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P26440 Isovaleryl-CoA dehydrogenase, mitochondrial
IVD
EC 1.3.8.4
NP_001152980.1 (Protein)
NM_001159508.1 (DNA/RNA sequence)
NP_002216.2 (Protein)
NM_002225.3 (DNA/RNA sequence)
PF00441 (Acyl-CoA_dh_1)
PF02770 (Acyl-CoA_dh_M)
PF02771 (Acyl-CoA_dh_N)
[Graphical View]

KEGG enzyme name
isovaleryl-CoA dehydrogenase
isovaleryl-coenzyme A dehydrogenase
isovaleroyl-coenzyme A dehydrogenase
3-methylbutanoyl-CoA:(acceptor) oxidoreductase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P26440 IVD_HUMAN Isovaleryl-CoA + electron-transfer flavoprotein = 3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein. Homotetramer. Mitochondrion matrix. FAD.

KEGG Pathways
Map code Pathways E.C.
MAP00280 Valine, leucine and isoleucine degradation

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00016 C02939 C04253 C03069 C04570
E.C.
Compound FAD 3-Methylbutanoyl-CoA Electron-transferring flavoprotein 3-Methylbut-2-enoyl-CoA Reduced electron-transferring flavoprotein
Type amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide amide group,carbohydrate,nucleotide ,peptide/protein,sulfide group amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,peptide/protein,phosphate group/phosphate ion amine group,carbohydrate,nucleotide ,peptide/protein,sulfide group amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,peptide/protein,phosphate group/phosphate ion
ChEBI 16238
15487
15486
PubChem 643975
165435
439855
439869
9549326
1ivhA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1ivhB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1ivhC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1ivhD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1ivhA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1ivhB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1ivhC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1ivhD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1ivhA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:COS Unbound Unbound Unbound
1ivhB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:COS Unbound Unbound Unbound
1ivhC03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:COS Unbound Unbound Unbound
1ivhD03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:COS Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P26440

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ivhA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ivhB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ivhC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ivhD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ivhA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ivhB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ivhC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ivhD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ivhA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 254
1ivhB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 254
1ivhC03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 254
1ivhD03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 254

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
Scheme 1, Scheme 4
[4]
p.8463

References
[1]
Resource
Comments ACTIVE SITE GLU-283.
Medline ID 95367542
PubMed ID 7640268
Journal Biochemistry
Year 1995
Volume 34
Pages 10146-52
Authors Mohsen AW, Vockley J
Title Identification of the active site catalytic residue in human isovaleryl-CoA dehydrogenase.
Related PDB
Related UniProtKB P26440
[2]
Resource
Comments
Medline ID
PubMed ID 8777688
Journal Arch Dis Child Fetal Neonatal Ed
Year 1996
Volume 74
Pages F211-3
Authors Lorek AK, Penrice JM, Cady EB, Leonard JV, Wyatt JS, Iles RA, Burns SP, Reynolds EO
Title Cerebral energy metabolism in isovaleric acidaemia.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 9201918
Journal Biochemistry
Year 1997
Volume 36
Pages 7761-8
Authors Schaller RA, Mohsen AW, Vockley J, Thorpe C
Title Mechanism-based inhibitor discrimination in the acyl-CoA dehydrogenases.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-421.
Medline ID 97361954
PubMed ID 9214289
Journal Biochemistry
Year 1997
Volume 36
Pages 8455-64
Authors Tiffany KA, Roberts DL, Wang M, Paschke R, Mohsen AW, Vockley J, Kim JJ
Title Structure of human isovaleryl-CoA dehydrogenase at 2.6 A resolution: structural basis for substrate specificity,.
Related PDB 1ivh
Related UniProtKB P26440
[5]
Resource
Comments
Medline ID
PubMed ID 9665741
Journal Biochemistry
Year 1998
Volume 37
Pages 10325-35
Authors Mohsen AW, Anderson BD, Volchenboum SL, Battaile KP, Tiffany K, Roberts D, Kim JJ, Vockley J
Title Characterization of molecular defects in isovaleryl-CoA dehydrogenase in patients with isovaleric acidemia.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 10713113
Journal J Biol Chem
Year 2000
Volume 275
Pages 7958-63
Authors Volchenboum SL, Vockley J
Title Mitochondrial import and processing of wild type and type III mutant isovaleryl-CoA dehydrogenase.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 11386848
Journal Mol Genet Metab
Year 2001
Volume 73
Pages 126-37
Authors Mohsen AW, Navarette B, Vockley J
Title Identification of Caenorhabditis elegans isovaleryl-CoA dehydrogenase and structural comparison with other acyl-CoA dehydrogenases.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 11592819
Journal Mol Genet Metab
Year 2001
Volume 74
Pages 226-37
Authors Volchenboum SL, Mohsen AW, Kim JJ, Vockley J
Title Arginine 387 of human isovaleryl-CoA dehydrogenase plays a crucial role in substrate/product binding.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the acyl-CoA dehydrogenase family.

Created Updated
2004-03-25 2012-10-03