Kinetic characterization of caffeoyl-coenzyme a-specific 3-o-methyltransferase from elicited parsley cell suspensions.
Identifieur interne : 002D00 ( Main/Exploration ); précédent : 002C99; suivant : 002D01Kinetic characterization of caffeoyl-coenzyme a-specific 3-o-methyltransferase from elicited parsley cell suspensions.
Auteurs : A E Pakusch [Allemagne] ; U. MaternSource :
- Plant physiology [ 0032-0889 ] ; 1991.
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.
DOI: 10.1104/pp.96.1.327
PubMed: 16668176
PubMed Central: PMC1080756
Affiliations:
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Matern</name></author></analytic><series><title level="j">Plant physiology</title><idno type="ISSN">0032-0889</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">16668176</PMID><DateCompleted><Year>2010</Year><Month>06</Month><Day>29</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>14</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0032-0889</ISSN><JournalIssue CitedMedium="Print"><Volume>96</Volume><Issue>1</Issue><PubDate><Year>1991</Year><Month>May</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>Kinetic characterization of caffeoyl-coenzyme a-specific 3-o-methyltransferase from elicited parsley cell suspensions.</ArticleTitle><Pagination><MedlinePgn>327-30</MedlinePgn></Pagination><Abstract><AbstractText>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. 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