Lactate dehydrogenase properties

Brown, A. T. and Wittenberger, C. L. 1972. Fructose 1,6 diphosphate-dependent lactate dehydrogenase from a cariogenic streptococcus Purification and regulatory properties. J. Bacteriol. 110, 604-615. 

Crow, F. L. and Pritchard, G. C. 1977. Fructose 1,6 diphosphate activated lactate dehydrogenase from Streptococcus lactis Kinetic properties and factors affecting activation. J. Bacteriol. 131, 82-91. 

The flavoenzyme D-lactate dehydrogenase from yeast has been reported to contain zinc (134). An apoenzyme can be prepared and reactivated by Zn2+ or Co2+ (135). When yeast is grown in the presence of added Co2+, a Co(II) enzyme is synthesized. The biosynthetic Co(II) enzyme was found to have different catalytic properties compared to the enzyme reactivated from the apoenzyme (136). Only rather fragmentary data have been published on this subject, and the differences in cobalt binding obtained by the two methods of preparation are unknown. 

Valkirs, A. (1978). Temperature and pH effects on catalytic properties of lactate dehydrogenase from pelagic fish. Comparative Biochemistry and Physiology 59A, 31-36. 

Isoenzymes Isoenzymes are different forms of an enzyme which catalyze the same reaction, but which exhibit different physical or kinetic properties. The isoenzymes of lactate dehydrogenase (LDH) can be separated electrophoretically and can be used clinically to diagnose a myocardial infarction. 

Holland, L.Z., M. McFall-Ngai, and G.N. Somero (1997). Evolution of lactate dehydrogenase-A homologs of barracuda fishes (genus Sphyraena) from different thermal environments Differences in kinetic properties and thermal stability are due to amino acid substitutions outside the active site. Biochemistry 36 3207-3215. 

Soluble D-lactate dehydrogenases with enzymic properties similar to those of the D-2-hydroxyacid dehydrogenase of anaerobic yeast have been isolated from rabbit kidney mitochondria (333-334) and from a species of Mycohacterium (335). It is not clear whether these enzymes are metal-containing flavoproteins. 

Lactate dehydrogenase(s), types of, 263 d(—)-Lactate dehydrogenase, 269-270 enzymic properties, 270-272 physical properties, 270 l(-I-)-Lactate dehydrogenase cytochrome bt core, 266-267 enzymic properties, 267-269 historical background, 263-264 physical properties, 264-266... 

Deng, H., Zheng, J., Burgner, J., and Callender, R., Molecular properties of pyruvate bound to lactate dehydrogenase A Raman spectroscopic study, Proc. Nat. Acad. Sci., USA 86, 4484-4488 (1989). 

Stefuca, V. Gemeiner, P. Kurillova, L. Dautzenberg, H. Polakovic, M. Bales, V. Polyelectrolyte complex capsulesas a material for enzyme immobilization, catalytic properties of encapsulated lactate dehydrogenase. Appl. Biochem. Biotechnol. 1991, 30 (3), 313-324. 

Labeyrie et al. (41) isolated a trypsin fragment of 11 kDa from S. cerevisiae flavocytochrome 62 that contained heme but was devoid of flavin and had no lactate dehydrogenase activity. The fragment, which was referred to as cytochrome 62 core, was found to have spectral properties very like those of microsomal cytochrome 65 (41). This similarity with cytochrome 65 is borne out by comparisons of amino acid sequence (42-44). The sequence similarity extends to related heme domains of sulfite oxidase (45, 46) and assimilatory nitrate reductase (47). The existence of a protein family with a common cytochrome 65 fold was suggested by Guiard and Lederer (48) and this is supported by the close similarity between the three-dimensional structures of microsomal cytochrome 65 (49) and the cytochrome domain of flavocytochrome 62 (23-25). 

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