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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 3
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pubmed:dateCreated |
2004-9-1
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pubmed:abstractText |
Magnesium protoporphyrin IX methyltransferase (ChlM), an enzyme in the chlorophyll biosynthetic pathway, catalyses the transfer of a methyl group to magnesium protoporphyrin IX (MgP) to form magnesium protoporphyrin IX monomethyl ester (MgPME). S-Adenosyl-L-methionine is the other substrate, from which a methyl group is transferred to the propionate group on ring C of the porphyrin macrocycle. Stopped-flow techniques were used to characterize the binding of porphyrin substrate to ChlM from Synechocystis PCC6803 by monitoring tryptophan fluorescence quenching on a millisecond timescale. We concluded that a rapid binding step is preceded by a slower isomerization of the enzyme. Quenched-flow techniques have been employed to characterize subsequent partial reactions in the catalytic mechanism. A lag phase has been identified that has been attributed to the formation of an intermediate. Our results provide a greater understanding of this catalytic process which controls the relative concentrations of MgP and MgPME, both of which are implicated in signalling between the plastid and nucleus in plants.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-10080885,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-10437802,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-10572128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-10671528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-11033354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-11115133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-11172074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-12357035,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-12489983,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-12511958,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-12574634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-1390649,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-1932026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-3056725,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-3558369,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-7690685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-7925960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-8071204,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-8573073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-8631364,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-9092496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-9391171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-9492312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-9716491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-9730838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-9852082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15239672-9882621
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1470-8728
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
382
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1009-13
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15239672-Chromatography, High Pressure Liquid,
pubmed-meshheading:15239672-Isomerism,
pubmed-meshheading:15239672-Kinetics,
pubmed-meshheading:15239672-Methyltransferases,
pubmed-meshheading:15239672-Models, Chemical,
pubmed-meshheading:15239672-Protein Binding,
pubmed-meshheading:15239672-Protoporphyrins,
pubmed-meshheading:15239672-Spectrometry, Fluorescence
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pubmed:year |
2004
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pubmed:articleTitle |
Transient kinetics of the reaction catalysed by magnesium protoporphyrin IX methyltransferase.
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pubmed:affiliation |
Robert Hill Institute for Photosynthesis and Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK. shepherd@secsg.uga.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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