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Butanediole dehydrogenase

Purification and Characterization of (5)-1,3-Butanediol Dehydrogenase from Candida parapsiiosis 225... [Pg.225]

Tab. 3 Purification of NAD+-dependent (S)-l,3-butanediol dehydrogenase from Candida parapsi-lopsis. Tab. 3 Purification of NAD+-dependent (S)-l,3-butanediol dehydrogenase from Candida parapsi-lopsis.
The oxidative reaction was carried out as described in Materials and Methods for (S)-l,3-butanediol dehydrogenase, except that substrates and cofactors indicated in the table were used. Activity for (S)-1,3-butanediol was taken as 100%. [Pg.226]

Ui S, Takusagawa Y, Ohtsuki T, Mimura A, Ohkuma M, Kudo T. (2001). Stereochemical applications of the expression of the L-2,3-butanediol dehydrogenase gene in Escherichia coli. Lett Appl Microbiol, 32, 93-98. [Pg.286]

Diacetyl synthase 2 acetoin dehydrogenase 3 d-(—)-butanediol dehydrogenase 4 acetolactate dehydrogenase 5 acetolactate synthase... [Pg.144]

Fig. 10.33. Formation of diacetyl and butanediol from citrate by Streptococci. 1 citratase, 2 oxaloac-etate decarboxylase, 3 pyruvate decarboxylase, 4 a-acetolactate synthase, 5 diacetyl reductase, 6 a-acetolactate decarboxylase, 7 2,3-butanediol dehydrogenase... Fig. 10.33. Formation of diacetyl and butanediol from citrate by Streptococci. 1 citratase, 2 oxaloac-etate decarboxylase, 3 pyruvate decarboxylase, 4 a-acetolactate synthase, 5 diacetyl reductase, 6 a-acetolactate decarboxylase, 7 2,3-butanediol dehydrogenase...
Three enzymes are involved in the synthesis of 2,3-BD a-acetolactate synthase (EC 4.1.3.18), a-acetolactate decarboxylase (EC 4.1.1.5), and butanediol dehydrogenase (also known as diacetyl [acetoin] reductase Larsen and Stormer 1973 Johansen et al. 1975 Stormer 1975). Two different enzymes form acetolactate from pyruvate. The first, termed catabolic a-acetolactate synthase, has a pH optimum of 5.8 in acetate and is part of the butanediol pathway. The other enzyme, termed anabolic a-acetolactate synthase or acetohydroxyacid synthetase, has been well studied and characterized and will not be discussed here. This enzyme is part of the biosynthetic pathway for isoleucine, leucine, and valine and is coded for by the ilvBN, ilvGM, and ilvH genes in E. colt and Salmonella typhimurium (Bryn and Stormer 1976). [Pg.120]

A novel mechanism for stereoisomer formation was described for Bacillus polymyxa. The RR-acetoin formed from pyruvate is converted into RR-butanediol by diacetyl (acetoin) reductase. The same enzyme reduces diacetyl to RR-acetoin. An S-acetoin-forming diacetyl reductase converts diacetyl to SS-acetoin. The racemic acetoin molecules are acted upon by a butanediol dehydrogenase, which generates either RR-butanediol or meso-butanediol (Ui et al. 1986). [Pg.120]

Taylor MB, Juni E (1960) Stereoisomeric specificities of 2,3-butanediol dehydrogenases. Biochim Biophys Acta 39 448—457 Terracciano JS, Kashket ER (1986) Intracellular conditions required of initiation of solvent production by Clostridium acetobutylicum. Appl Environ... [Pg.132]

Figure 1.2. Citrate metabolism in Lactococcus, Leuconostoc, and Weissella species. Key for the enzymes CL, citrate lyase OAD, oxaloacetate decarboxylase LDH, lactate dehydrogenase PDC, pyruvate decarboxylase ALS, a-acetolactate synthase ADC, a-acetolactate decarboxylase DAR, diacetyl acetoln reductase BDH, 2,3-butanediol dehydrogenase Tppi, thiamine pyrophosphate. Figure 1.2. Citrate metabolism in Lactococcus, Leuconostoc, and Weissella species. Key for the enzymes CL, citrate lyase OAD, oxaloacetate decarboxylase LDH, lactate dehydrogenase PDC, pyruvate decarboxylase ALS, a-acetolactate synthase ADC, a-acetolactate decarboxylase DAR, diacetyl acetoln reductase BDH, 2,3-butanediol dehydrogenase Tppi, thiamine pyrophosphate.

See other pages where Butanediole dehydrogenase is mentioned: [Pg.85]    [Pg.320]    [Pg.161]    [Pg.398]    [Pg.271]    [Pg.206]    [Pg.3]    [Pg.100]    [Pg.149]    [Pg.124]    [Pg.2]    [Pg.392]   
See also in sourсe #XX -- [ Pg.144 ]




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