チオホラーゼ
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/04/16 23:14:19」(JST)
[Wiki en表示]
3-Hydroxybutyrate dehydrogenase |
Identifiers |
EC number |
1.1.1.30 |
CAS number |
9028-38-0 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Gene Ontology |
AmiGO / EGO |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
|
In enzymology, a 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) is an enzyme that catalyzes the chemical reaction
- (R)-3-hydroxybutanoate + NAD+ acetoacetate + NADH + H+
Thus, the two substrates of this enzyme are (R)-3-hydroxybutanoate and NAD+, whereas its three products are acetoacetate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-3-hydroxybutanoate:NAD+ oxidoreductase. Other names in common use include NAD+-beta-hydroxybutyrate dehydrogenase, hydroxybutyrate oxidoreductase, beta-hydroxybutyrate dehydrogenase, D-beta-hydroxybutyrate dehydrogenase, D-3-hydroxybutyrate dehydrogenase, D-(–)-3-hydroxybutyrate dehydrogenase, beta-hydroxybutyric acid dehydrogenase, 3-D-hydroxybutyrate dehydrogenase, and beta-hydroxybutyric dehydrogenase. This enzyme participates in synthesis and degradation of ketone bodies and butanoate metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1WMB and 1X1T.
See also
References
- Bergmeyer HU, Gawehn K, Klotzsch H, Krebs HA, Williamson DH (1967). "Purification and properties of crystalline 3-hydroxybutyrate dehydrogenase from Rhodopseudomonas spheroides". Biochem. J. 102 (2): 423–31. PMC 1270263. PMID 4291491.
- Delafield FP, Cooksey KE, Doudoroff M (1965). "beta-Hydroxybutyric dehydrogenase and dimer hydrolase of Pseudomonas lemoignei". J. Biol. Chem. 240 (10): 4023–8. PMID 4954074.
- Lehninger AL, Sudduth HC and Wise JB (1960). "D-beta-Hydroxybutyric dehydrogenase of mitochondria". J. Biol. Chem. 235: 2450–2455. PMID 14415394.
English Journal
- A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency.
- Shafqat N, Kavanagh KL, Sass JO, Christensen E, Fukao T, Lee WH, Oppermann U, Yue WW.SourceStructural Genomics Consortium, University of Oxford, Oxford, OX3 7DQ, UK.
- Journal of inherited metabolic disease.J Inherit Metab Dis.2013 Nov;36(6):983-7. doi: 10.1007/s10545-013-9589-z. Epub 2013 Feb 19.
- Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency is a rare inherited metabolic disorder of ketone metabolism, characterized by ketoacidotic episodes and often permanent ketosis. To date there are ∼20 disease-associated alleles on the OXCT1 gene that encodes the mitochondrial enzyme SCOT.
- PMID 23420214
- Structure of succinyl-CoA:3-ketoacid CoA transferase from Drosophila melanogaster.
- Zhang M, Xu HY, Wang YC, Shi ZB, Zhang NN.SourceSchool of Life Science, Anhui University, Hefei 230026, People's Republic of China.
- Acta crystallographica. Section F, Structural biology and crystallization communications.Acta Crystallogr Sect F Struct Biol Cryst Commun.2013 Oct;69(Pt 10):1089-93. doi: 10.1107/S1744309113024986. Epub 2013 Sep 28.
- Succinyl-CoA:3-ketoacid CoA transferase (SCOT) plays a crucial role in ketone-body metabolism. SCOT from Drosophila melanogaster (DmSCOT) was purified and crystallized. The crystal structure of DmSCOT was determined at 2.64 Å resolution and belonged to space group P212121, with unit-cell paramete
- PMID 24100554
- Impact of peripheral ketolytic deficiency on hepatic ketogenesis and gluconeogenesis during the transition to birth.
- Cotter DG, Ercal B, d'Avignon DA, Dietzen DJ, Crawford PA.SourceDepartment of Medicine, Washington University, St Louis, Missouri 63110, USA.
- The Journal of biological chemistry.J Biol Chem.2013 Jul 5;288(27):19739-49. doi: 10.1074/jbc.M113.454868. Epub 2013 May 20.
- Preservation of bioenergetic homeostasis during the transition from the carbohydrate-laden fetal diet to the high fat, low carbohydrate neonatal diet requires inductions of hepatic fatty acid oxidation, gluconeogenesis, and ketogenesis. Mice with loss-of-function mutation in the extrahepatic mitocho
- PMID 23689508
Related Links
- thiophorase An obsolete, generic term for any of the coenzyme-A transferases. ... Disclaimer All content on this website, including dictionary, thesaurus, literature, geography, and other reference data is for informational purposes ...
- Learn and talk about Thiophorase , and check out Thiophorase on Wikipedia, Youtube, Google News, Google Books, and Twitter on ...
Related Pictures
★リンクテーブル★
[★]
- 英
- thiophorase
- 同
- succinyl-CoA-acetoacetate-CoA transferase
[show details]
[★]
- 同
- thiophorase, succinyl CoA:acetoacetate CoA-transferase, succinyl-CoA acetoacetate CoA transferase