Production of racemic lactic acid in Pediococcus cerevisiae cultures by two lactate dehydrogenases

Gordon G.L. and Doelle H.W. (1975) Production of racemic lactic acid in Pediococcus cerevisiae cultures by two lactate dehydrogenases. Journal of Bacteriology, 121 2: 600-607.

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Author Gordon G.L.
Doelle H.W.
Title Production of racemic lactic acid in Pediococcus cerevisiae cultures by two lactate dehydrogenases
Formatted title
Production of racemic lactic acid in Pediococcus cerevisiae cultures by two lactate dehydrogenases
Journal name Journal of Bacteriology   Check publisher's open access policy
ISSN 0021-9193
1098-5530
Publication date 1975-02
Sub-type Article (original research)
Open Access Status File (Publisher version)
Volume 121
Issue 2
Start page 600
End page 607
Total pages 8
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Language eng
Formatted abstract
Nicotinamide adenine dinucleotide (NAD) dependent D(-) and L(+) lactate dehydrogenases have been partially purified 89 and 70 fold simultaneously from cell free extracts of P. cerevisiae. Native molecular weights, as estimated from molecular sieve chromatography and electrophoresis in non denaturing polyacrylamide gels, are 71,000 to 73,000 for D(-) lactate dehydrogenase and 136,000 to 139,000 for L(+) lactate dehydrogenase. Electrophoresis in sodium dodecyl sulfate containing gels reveals subunits with approximate molecular weights of 37,000 to 39,000 for both enzymes. By lowering the pyruvate concentration from 5.0 to 0.5 mM, the pH optimum for pyruvate reduction by D(-) lactate dehydrogenase decreases from pH 8.0 to 3.6. However, L(+) lactate dehydrogenase displays an optimum for pyruvate reduction between pH 4.5 and 6.0 regardless of the pyruvate concentration. The enzymes obey Michaelis Menten kinetics for both pyruvate and reduced NAD at pH 5.4 and 7.4 with increased affinity for both substrates at the acid pH. α Ketobutyrate can be used as a reducible substrate, whereas oxamate has no inhibitory effect on lactate oxidation by either enzyme. Adenosine triphosphate causes inhibition of both enzymes by competition with reduced NAD. Adenosine diphosphate is also inhibitory under the same conditions, whereas NAD acts as a product inhibitor. The results are discussed with relation to the lactate isomer production during the growth cycle of P. cerevisiae.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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