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. 1968 Nov;43(11):1813–1820. doi: 10.1104/pp.43.11.1813

Comparative Studies of Enzymes Related to Serine Metabolism in Higher Plants 1

Geoffrey P Cheung 1,2, I Y Rosenblum 1,3, H J Sallach 1
PMCID: PMC1087083  PMID: 5699148

Abstract

The following enzymes related to serine metabolism in higher plants have been investigated: 1) d-3-phosphoglycerate dehydrogenase, 2) phosphohydroxypyruvate:l-glutamate transaminase, 3) d-glycerate dehydrogenase, and 4) hydroxypyruvate:l-alanine transaminase. Comparative studies on the distribution of the 2 dehydrogenases in seeds and leaves from various plants revealed that d-3-phosphoglycerate dehydrogenase is widely distributed in seeds in contrast to d-glycerate dehydrogenase, which is either absent or present at low levels, and that the reverse pattern is observed in green leaves.

The levels of activity of the 4 enzymes listed above were followed in different tissues of the developing pea (Pisum sativum, var. Alaska). In the leaf, from the tenth to seventeenth day of germination, the specific activity of d-glycerate dehydrogenase increased markedly and was much higher than d-3-phosphoglycerate dehydrogenase which remained relatively constant during this time period. Etiolation resulted in a decrease in d-glycerate dehydrogenase and an increase in d-3-phosphoglycerate dehydrogenase activities. In apical meristem, on the other hand, the level of d-3-phosphoglycerate dehydrogenase exceeded that of d-glycerate dehydrogenase at all time periods studied. Low and decreasing levels of both dehydrogenases were found in epicotyl and cotyledon. The specific activities of the 2 transaminases remained relatively constant during development in both leaf and apical meristem. In general, however, the levels of phosphohydroxypyruvate:l-glutamate transaminase were comparable to those of d-3-phosphoglycerate dehydrogenase in a given tissue as were those for hydroxypyruvate: l-alanine transaminase and d-glycerate dehydrogenase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. CANVIN D. T., BEEVERS H. Sucrose synthesis from acetate in the germinating castor bean: kinetics and pathway. J Biol Chem. 1961 Apr;236:988–995. [PubMed] [Google Scholar]
  2. Chang W. H., Tolbert N. E. Distribution of C in Serine and Glycine after CO(2) Photosynthesis by Isolated Chloroplasts. Modification of Serine-C Degradation. Plant Physiol. 1965 Nov;40(6):1048–1052. doi: 10.1104/pp.40.6.1048. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Fallon H. J., Byrne W. L. 2-phosphoglyceric acid phosphatase: identification and properties of the beef-liver enzyme. Biochim Biophys Acta. 1965 Jul 29;105(1):43–53. doi: 10.1016/s0926-6593(65)80174-6. [DOI] [PubMed] [Google Scholar]
  4. GREENBERG D. M., ICHIHARA A. Further studies on the pathway of serine formation from carbohydrate. J Biol Chem. 1957 Jan;224(1):331–340. [PubMed] [Google Scholar]
  5. Gientka-Rychter A., Cherry J. H. De Novo Synthesis of Isocitritase in Peanut (Arachis hypogaea L.) Cotyledons. Plant Physiol. 1968 Apr;43(4):653–659. doi: 10.1104/pp.43.4.653. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. HOLZER H., HOLLDORF A. Isolierung von D-Glycerat-dehydrogenase, einige Eigenschaften des Enzyms und seine Verwendung zur enzymatisch-optischen Bestimmung von Hydroxypyruvat neben Pyruvat. Biochem Z. 1957;329(4):292–312. [PubMed] [Google Scholar]
  7. Hess J. L., Tolbert N. E. Glycolate pathway in algae. Plant Physiol. 1967 Mar;42(3):371–379. doi: 10.1104/pp.42.3.371. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hess J. L., Tolbert N. E. Glycolate, glycine, serine, and glycerate formation during photosynthesis by tobacco leaves. J Biol Chem. 1966 Dec 10;241(23):5705–5711. [PubMed] [Google Scholar]
  9. LAMPRECHT W., DIAMANTSTEIN T., HEINZ F., BALDE P. [Phosphorylation of D-glyceric acid to 2-phospho-D-glyceric acid with glycerate kinase in the liver. I. On the biochemistry of fructose metabolism. II]. Hoppe Seylers Z Physiol Chem. 1959 Sep 30;316:97–112. doi: 10.1515/bchm2.1959.316.1.97. [DOI] [PubMed] [Google Scholar]
  10. LAMPRECHT W., HEINZ F. Isolierung von Glycerinaldehyd-Dehydrogenase aus Rattenleber; zur Biochemie des Fructosestoffwechsels. Z Naturforsch B. 1958 Jul;13B(7):464–465. [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. Longo C. P. Evidence for de novo synthesis of isocitratase and malate synthesis in germinating peanut cotyledons. Plant Physiol. 1968 Apr;43(4):660–664. doi: 10.1104/pp.43.4.660. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. MEISTER A. Enzymatic preparation of alpha-keto acids. J Biol Chem. 1952 May;197(1):309–317. [PubMed] [Google Scholar]
  14. RABSON R., TOLBERTNE, KEARNEY P. C. Formation of serine and glyceric acid by the glycolate pathway. Arch Biochem Biophys. 1962 Jul;98:154–163. doi: 10.1016/0003-9861(62)90161-3. [DOI] [PubMed] [Google Scholar]
  15. Stafford H. A., Magaldi A. A Developmental Study of D-Glyceric Acid Dehydrogenase. Plant Physiol. 1954 Nov;29(6):504–508. doi: 10.1104/pp.29.6.504. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Walsh D. A., Sallach H. J. Comparative studies on the pathways for serine biosynthesis in animal tissues. J Biol Chem. 1966 Sep 10;241(17):4068–4076. [PubMed] [Google Scholar]

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