1887

Abstract

Extracts of contain NADP-linked hydroxypyruvate reductase activity. The enzyme responsible has been separated and partially purified. It showed some activity with glyoxylate, acetoin, diacetyl and oxaloacetate and was 2 1/2 times as active with NADP as with NAD. It appears to be a constitutive enzyme and possible metabolic roles for it are discussed. Attention is drawn to the dangers of relying solely on the presence of hydroxypyruvate reductase as a diagnostic marker for the operation of a serine pathway of C-assimilation in a micro-organism. The malate dehydrogenase from has been partially purified and shown to possess no glycerate dehydrogenase or hydroxypyruvate reductase activity.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-101-2-259
1977-08-01
2021-08-01
Loading full text...

Full text loading...

/deliver/fulltext/micro/101/2/mic-101-2-259.html?itemId=/content/journal/micro/10.1099/00221287-101-2-259&mimeType=html&fmt=ahah

References

  1. Blackmore M. A., Quayle J. R. 1970; Microbial growth on oxalate by a route not involving glyoxylate carboligase. Biochemical Journal 118:53–59
    [Google Scholar]
  2. Cox R. B., Quayle J. R. 1975; The autotrophic growth of Micrococcus denitrificans on methanol. Biochemical Journal 150:569–571
    [Google Scholar]
  3. Davis B. J. 1964; Disc electrophoresis. Methods and application to human serum proteins. Annals of the New York Academy of Sciences 121:404–427
    [Google Scholar]
  4. Dawson R. M. C., Elliott D. C., Elliott W. H., Jones K. M. 1969 Data for Biochemical Research, 2nd edn.. Oxford: Clarendon Press;
    [Google Scholar]
  5. Dixon M. 1953a; A nomogram for ammonium sulphate solutions. Biochemical Journal 54:457–458
    [Google Scholar]
  6. Dixon M. 1953b; The determination of enzyme inhibitor constants. Biochemical Journal 55:170–171
    [Google Scholar]
  7. Eisenthal R., Cornish-Bowden A. 1974; The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters. Biochemical Journal 139:715–720
    [Google Scholar]
  8. Fraenkel D. G., Vinopal R. T. 1973; Carbohydrate metabolism in bacteria. Annual Review of Microbiology 27:69–100
    [Google Scholar]
  9. Gibbs R. G. 1966 The enzymology of the β-hydroxyaspartate pathway. Ph.D. thesis University of Leicester:
    [Google Scholar]
  10. Harder W., Quayle J. R. 1971a; The biosynthesis of serine and glycine in Pseudomonas AM1 with special reference to growth on carbon sources other than C1 compounds. Biochemical Journal 121:753–762
    [Google Scholar]
  11. Harder W., Quayle J. R. 1971b; Aspects of glycine and serine biosynthesis during growth of Pseudomonas AM1 on C1 compounds. Biochemical Journal 121:763–769
    [Google Scholar]
  12. Heptinstall J., Quayle J. R. 1970; Pathways leading to and from serine during growth of Pseudomonas AM1 on C1 compounds or succinate. Biochemical Journal 117:563–572
    [Google Scholar]
  13. Hirsch-Kolb H., Greenberg D. M. 1971; Phosphoserine aminotransferase (sheep brain). Methods in Enzymology 17B:331–334
    [Google Scholar]
  14. Kato N., Tsuji K., Ohashi H., Tani Y., Ogata K. 1977; The assimilation pathways of C1-compounds in Streptomyces sp. No. 239 during growth on methanol. Agricultural and Biological Chemistry 41:29–34
    [Google Scholar]
  15. Kohn L. D., Jakoby W. B. 1968a; Tartaric acid metabolism. III. The formation of glyceric acid. Journal of Biological Chemistry 243:2465–2471
    [Google Scholar]
  16. Kohn L. D., Jakoby W. B. 1968b; Tartaric acid metabolism. VII. Crystalline hydroxypyruvate reductase (d-glycerate dehydrogenase). Journal of Biological Chemistry 243:2494–2499
    [Google Scholar]
  17. Kornberg H. L. 1966; Anaplerotic sequences and their role in metabolism. Essays in Biochemistry 2:1–31
    [Google Scholar]
  18. Kornberg H. L., Morris J. G. 1965; The utilization of glycollate by Micrococcus denitrificans: the β-hydroxyaspartate pathway. Biochemical Journal 95:577–586
    [Google Scholar]
  19. Large P. J., Carter R. H. 1973; Specific activities of enzymes of the serine pathway of carbon assimilation in Pseudomonas aminovorans and Pseudomonas ms grown on methylamine. Biochemical Society Transactions 1:1291–1293
    [Google Scholar]
  20. Large P. J., Quayle J. R. 1963; Microbial growth on C1 compounds. Enzyme activities in extracts of Pseudomonas AMI. Biochemical Journal 87:386–396
    [Google Scholar]
  21. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  22. Pizer C. I., Sugimoto E. l97l; 3-Phosphoglycerate dehydrogenase (Escherichia coli). Methods in Enzymology 17B:325–331
    [Google Scholar]
  23. Quayle J. R. 1972; The metabolism of one-carbon compounds by micro-organisms. Advances in Microbial Physiology 7:119–203
    [Google Scholar]
  24. Willis J. E., Sallach H. J. 1962; Evidence for a mammalian d-glyceric dehydrogenase. Journal of Biological Chemistry 237:910–915
    [Google Scholar]
  25. Wood W. A. 1972; 2-Keto-3-deoxy-6-phosphogluconic and related aldolases. In The Enzymes, 3rd edn.. 7 pp. 281–302 Boyer P. D. Edited by New York & London: Academic Press;
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-101-2-259
Loading
/content/journal/micro/10.1099/00221287-101-2-259
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error