関: hydroxybutyrate dehydrogenase

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/12/01 20:36:55」(JST)

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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 3 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.

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. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1270263/.
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.

This EC 1.1.1 enzyme-related article is a stub. You can help Wikipedia by expanding it.

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English Journal

Increased NADPH availability in Escherichia coli: improvement of the product per glucose ratio in reductive whole-cell biotransformation.

Siedler S, Bringer S, Bott M.SourceInstitut für Bio- und Geowissenschaften, IBG-1: Biotechnologie, Forschungszentrum Jülich, 52425, Jülich, Germany.
Applied microbiology and biotechnology.Appl Microbiol Biotechnol.2011 Dec;92(5):929-37. Epub 2011 Jun 14.
A basic requirement for the efficiency of reductive whole-cell biotransformations is the reducing capacity of the host. Here, the pentose phosphate pathway (PPP) was applied for NADPH regeneration with glucose as the electron-donating co-substrate using Escherichia coli as host. Reduction of the pro
PMID 21670981

The effects of different environmental conditions on thermoregulation and clinical and hematological parameters in long-distance road-transported calves.

Bernardini D, Gerardi G, Peli A, Nanni Costa L, Amadori M, Segato S.SourceDepartment of Veterinary Clinical Sciences, University of Padova, 35020 Legnaro (PD), Italy.
Journal of animal science.J Anim Sci.2011 Nov 18. [Epub ahead of print]
The aim of this study was to investigate the effects of long-distance road transport (19 h, from Poland to Italy) during 2 seasons (summer vs. winter) on clinical and hematological parameters in calves. The environmental temperature range that could compromise the calves' thermoregulation system (th
PMID 22100587

Japanese Journal

Aerobic utilization of crude glycerol by recombinant Escherichia coli for simultaneous production of poly 3-hydroxybutyrate and bioethanol

Shah Pramod,Chiu Feng-Shen,Lan John Chi-Wei
Journal of bioscience and bioengineering 117(3), 343-350, 2014-03
NAID 40020024059

Aerobic utilization of crude glycerol by recombinant Escherichia coli for simultaneous production of poly 3-hydroxybutyrate and bioethanol(BIOCHEMICAL ENGINEERING)

Shah Pramod,Chiu Feng-Shen,Lan John Chi-Wei
Journal of bioscience and bioengineering 117(3), 343-350, 2014-03
… coli strains were constructed for the simultaneous production of poly 3-hydroxybutyrate (P3HB) and bioethanol from crude glycerol. … The incorporation of aldehyde reductase (Alrd) and aldehyde dehydrogenase (AldH) in recombinant strain showed 2-fold increment in crude glycerol utilization under aerobic condition. … Subsequently, acetate was utilized as substrate in the second pathway, which directly converted acetyl-CoA to P3HB. …
NAID 110009815388

Modification of β-oxidation pathway in Ralstonia eutropha for production of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) from soybean oil(MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)

Insomphun Chayatip,Mifune Jun,Orita Izumi [他],Numata Keiji,Nakamura Satoshi,Fukui Toshiaki
Journal of bioscience and bioengineering 117(2), 184-190, 2014-02
… This study focused on bifunctional (S)-specific 2-enoyl-CoA hydratase/(S)-3-hydroxyacyl-CoA dehydrogenase encoded byfadB to obtain information regarding β-oxidation in this bacterium and to achieve compositional regulation of poly((R)-3-hydroxybutyrate-co-(R)-3-hydroxyhexanoate) [P(3HB-co-3HHx)] synthesized from soybean oil. …
NAID 110009804070

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リンク元	「hydroxybutyrate dehydrogenase」「3-ヒドロキシ酪酸脱水素酵素」
関連記事	「hydroxybutyrate dehydrogenase」「dehydrogenase」「dehydrogenases」

「hydroxybutyrate dehydrogenase」

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 Protein	search