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 1.3.99.10 |
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 16238 |
15487 15487 |
15486 15486 |
||||||||
| PubChem |
643975 643975 |
165435 439855 165435 439855 |
439869 9549326 439869 9549326 |
||||||||
| 1ivhA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1ivhB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1ivhC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1ivhD01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1ivhA02 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | |
| 1ivhB02 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | |
| 1ivhC02 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | |
| 1ivhD02 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | |
| 1ivhA03 |
|
|
|
|
|
Unbound | Analogue:COS | Unbound | Unbound | Unbound | |
| 1ivhB03 |
|
|
|
|
|
Unbound | Analogue:COS | Unbound | Unbound | Unbound | |
| 1ivhC03 |
|
|
|
|
|
Unbound | Analogue:COS | Unbound | Unbound | Unbound | |
| 1ivhD03 |
|
|
|
|
|
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 |
|
|
|
|
|
|||||
| 1ivhB01 |
|
|
|
|
|
|||||
| 1ivhC01 |
|
|
|
|
|
|||||
| 1ivhD01 |
|
|
|
|
|
|||||
| 1ivhA02 |
|
|
|
|
|
|||||
| 1ivhB02 |
|
|
|
|
|
|||||
| 1ivhC02 |
|
|
|
|
|
|||||
| 1ivhD02 |
|
|
|
|
|
|||||
| 1ivhA03 |
|
|
|
|
|
GLU 254 | ||||
| 1ivhB03 |
|
|
|
|
|
GLU 254 | ||||
| 1ivhC03 |
|
|
|
|
|
GLU 254 | ||||
| 1ivhD03 |
|
|
|
|
|
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 |