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. 1991 May;96(1):327–330. doi: 10.1104/pp.96.1.327

Kinetic Characterization of Caffeoyl-Coenzyme A-Specific 3-O-Methyltransferase from Elicited Parsley Cell Suspensions 1

Anne-Elisabeth Pakusch 1, Ulrich Matern 1
PMCID: PMC1080756  PMID: 16668176

Abstract

The activity of caffeoyl-coenzyme A (CoA) 3-O-methyltransferase, an enzyme widely distributed in plants and involved in cell wall reinforcement in a disease resistance response, appears to be subject to a complex type of regulation in vivo. In cultured parsley (Petroselinum crispum) cells treated with an elicitor from Phytophthora megasperma f.sp. glycinea, the enzyme activity is rapidly induced by a transient increase in the rate of de novo transcription. Parsley caffeoyl-CoA-specific methyltransferase differs in several aspects from other plant O-methyltransferases but shows limited homology to bacterial adenine-specific DNA methyltransferases. Kinetic analysis revealed an Ordered Bi Bi mechanism for catalysis, with caffeoyl-CoA bound prior to S-adenosyl-l-methionine and feruloyl-CoA released last from the enzyme. The small inhibitory constant determined in vitro for feruloyl-CoA suggests that, in vivo, the enzyme activity is also under tight control by the steady-state product concentration in addition to the rate of transcription that becomes affected upon elicitor challenge.

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Selected References

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

  1. CLELAND W. W. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory. Biochim Biophys Acta. 1963 Feb 12;67:173–187. doi: 10.1016/0006-3002(63)91815-8. [DOI] [PubMed] [Google Scholar]
  2. De Luca V., Ibrahim R. K. Enzymatic synthesis of polymethylated flavonols in Chrysosplenium americanum. II. Substrate interaction and product inhibition studies of flavonol 3-, 6-, and 4'-O-methyltransferases. Arch Biochem Biophys. 1985 May 1;238(2):606–618. doi: 10.1016/0003-9861(85)90206-1. [DOI] [PubMed] [Google Scholar]
  3. Flohe L., Schwabe K. P. Kinetics of purified catechol O-methyltransferase. Biochim Biophys Acta. 1970 Dec 16;220(3):469–476. doi: 10.1016/0005-2744(70)90278-0. [DOI] [PubMed] [Google Scholar]
  4. Hermann C., Legrand M., Geoffroy P., Fritig B. Enzymatic synthesis of lignin: purification to homogeneity of the three O-methyltransferases of tobacco and production of specific antibodies. Arch Biochem Biophys. 1987 Mar;253(2):367–376. doi: 10.1016/0003-9861(87)90190-1. [DOI] [PubMed] [Google Scholar]
  5. Ingrosso D., Fowler A. V., Bleibaum J., Clarke S. Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. Common sequence motifs for protein, DNA, RNA, and small molecule S-adenosylmethionine-dependent methyltransferases. J Biol Chem. 1989 Nov 25;264(33):20131–20139. [PubMed] [Google Scholar]
  6. Khouri H. E., Tahara S., Ibrahim R. K. Partial purification, characterization, and kinetic analysis of isoflavone 5-O-methyltransferase from yellow lupin roots. Arch Biochem Biophys. 1988 May 1;262(2):592–598. doi: 10.1016/0003-9861(88)90410-9. [DOI] [PubMed] [Google Scholar]
  7. Knogge W., Weissenböck G. Purification, characterization, and kinetic mechanism of S-adenosyl-L-methionine: vitexin 2"-O-rhamnoside 7-O-methyltransferase of Avena sativa L. Eur J Biochem. 1984 Apr 2;140(1):113–118. doi: 10.1111/j.1432-1033.1984.tb08073.x. [DOI] [PubMed] [Google Scholar]
  8. Lauster R. Evolution of type II DNA methyltransferases. A gene duplication model. J Mol Biol. 1989 Mar 20;206(2):313–321. doi: 10.1016/0022-2836(89)90481-6. [DOI] [PubMed] [Google Scholar]
  9. Pakusch A. E., Matern U., Schiltz E. Elicitor-Inducible Caffeoyl-Coenzyme A 3-O-Methyltransferase from Petroselinum crispum Cell Suspensions : Purification, Partial Sequence, and Antigenicity. Plant Physiol. 1991 Jan;95(1):137–143. doi: 10.1104/pp.95.1.137. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Stöckigt J., Zenk M. H. Chemical syntheses and properties of hydroxycinnamoyl-coenzyme A derivatives. Z Naturforsch C. 1975 May-Jun;30(3):352–358. doi: 10.1515/znc-1975-5-609. [DOI] [PubMed] [Google Scholar]
  11. WILKINSON G. N. Statistical estimations in enzyme kinetics. Biochem J. 1961 Aug;80:324–332. doi: 10.1042/bj0800324. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Yee W. C., Eglsaer S. J., Richards W. R. Confirmation of a ping-pong mechanism for S-adenosyl-L-methionine:magnesium protoporphyrin methyltransferase of etiolated wheat by an exchange reaction. Biochem Biophys Res Commun. 1989 Jul 14;162(1):483–490. doi: 10.1016/0006-291x(89)92023-8. [DOI] [PubMed] [Google Scholar]

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