The Enzyme Database

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EC 1.1.5.1      
Deleted entry:  cellobiose dehydrogenase (quinone). Now known to be proteolytic product of EC 1.1.99.18, cellobiose dehydrogenase (acceptor)
[EC 1.1.5.1 created 1983, deleted 2002]
 
 
EC 1.1.5.10     
Accepted name: D-2-hydroxyacid dehydrogenase (quinone)
Reaction: (R)-2-hydroxyacid + a quinone = 2-oxoacid + a quinol
Other name(s): (R)-2-hydroxy acid dehydrogenase; (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase; D-lactate dehydrogenase (ambiguous)
Systematic name: (R)-2-hydroxyacid:quinone oxidoreductase
Comments: The enzyme from mammalian kidney contains one mole of FAD per mole of enzyme.(R)-lactate, (R)-malate and meso-tartrate are good substrates. Ubiquinone-1 and the dye 2,6-dichloroindophenol can act as acceptors; NAD+ and NADP+ are not acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Tubbs, P.K. and Greville, G.D. Dehydrogenation of D-lactate by a soluble enzyme from kidney mitochondria. Biochim. Biophys. Acta 34 (1959) 290–291. [DOI] [PMID: 13839714]
2.  Tubbs, P.K. and Greville, G.D. The oxidation of D-α-hydroxy acids in animal tissues. Biochem. J. 81 (1961) 104–114. [PMID: 13922962]
3.  Cammack, R. Assay, purification and properties of mammalian D-2-hydroxy acid dehydrogenase. Biochem. J. 115 (1969) 55–64. [PMID: 5359443]
4.  Cammack, R. D-2-hydroxy acid dehydrogenase from animal tissue. Methods Enzymol. 41 (1975) 323–329. [DOI] [PMID: 236454]
[EC 1.1.5.10 created 2014]
 
 
EC 1.1.5.11     
Accepted name: 1-butanol dehydrogenase (quinone)
Reaction: butan-1-ol + a quinone = butanal + a quinol
Other name(s): BOH
Systematic name: butan-1-ol:quinone oxidoreductase
Comments: This periplasmic quinoprotein alcohol dehydrogenase, characterized from the bacterium Thauera butanivorans, is involved in butane degradation. It contains a pyrroloquinoline quinone (PQQ) prosthetic group. cf. EC 1.1.2.9, 1-butanol dehydrogenase (cytochrome c).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vangnai, A.S., Arp, D.J. and Sayavedra-Soto, L.A. Two distinct alcohol dehydrogenases participate in butane metabolism by Pseudomonas butanovora. J. Bacteriol. 184 (2002) 1916–1924. [DOI] [PMID: 11889098]
2.  Vangnai, A.S., Sayavedra-Soto, L.A. and Arp, D.J. Roles for the two 1-butanol dehydrogenases of Pseudomonas butanovora in butane and 1-butanol metabolism. J. Bacteriol. 184 (2002) 4343–4350. [DOI] [PMID: 12142403]
[EC 1.1.5.11 created 2016]
 
 
EC 1.1.5.12     
Accepted name: D-lactate dehydrogenase (quinone)
Reaction: (R)-lactate + a quinone = pyruvate + a quinol
Other name(s): dld (gene name)
Systematic name: (R)-lactate:quinone 2-oxidoreductase
Comments: The enzyme is an FAD-dependent peripheral membrane dehydrogenase that participates in respiration. Electrons derived from D-lactate oxidation are transferred to the membrane soluble quinone pool.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kohn, L.D. and Kaback, H.R. Mechanisms of active transport in isolated bacterial membrane vesicles. XV. Purification and properties of the membrane-bound D-lactate dehydrogenase from Escherichia coli. J. Biol. Chem. 248 (1973) 7012–7017. [PMID: 4582730]
2.  Futai, M. Membrane D-lactate dehydrogenase from Escherichia coli. Purification and properties. Biochemistry 12 (1973) 2468–2474. [PMID: 4575624]
3.  Matsushita, K. and Kaback, H.R. D-lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome o oxidase. Biochemistry 25 (1986) 2321–2327. [PMID: 3013300]
4.  Peersen, O.B., Pratt, E.A., Truong, H.T., Ho, C. and Rule, G.S. Site-specific incorporation of 5-fluorotryptophan as a probe of the structure and function of the membrane-bound D-lactate dehydrogenase of Escherichia coli: a 19F nuclear magnetic resonance study. Biochemistry 29 (1990) 3256–3262. [PMID: 2185834]
5.  Dym, O., Pratt, E.A., Ho, C. and Eisenberg, D. The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme. Proc. Natl. Acad. Sci. USA 97 (2000) 9413–9418. [DOI] [PMID: 10944213]
[EC 1.1.5.12 created 2017]
 
 


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