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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
1987-6-9
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pubmed:abstractText |
Myristoyl CoA:protein N-myristoyltransferase (NMT) catalyzes the addition of myristic acid to the amino-terminal glycine residues of a number of eukaryotic proteins. Recently, we developed a cell-free system for analyzing NMT activity and have begun to characterize the substrate specificity of this enzyme by using a series of synthetic peptides. We have now purified NMT from Saccharomyces cerevisiae to apparent homogeneity. The native enzyme is a 55-kDa protein, exhibits no requirement for divalent cation, and appears to contain a histidine residue critical for enzyme activity. A total of 42 synthetic peptides have been used to define structure/activity relationships in NMT substrates. An amino-terminal glycine is required for acylation; substitution with glycine analogues produces peptides that are inactive as substrates or inhibitors of NMT. A broad spectrum of amino acids is permitted at positions 3 and 4, while strict amino acid requirements are exhibited at position 5. Replacement of Ala5 in the peptide Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg with Asp ablates the peptide's myristoyl-accepting activity. A serine at this position results in a decrease by a factor of approximately equal to 500 in the apparent Km in the context of three different sequences. Penta- and hexa-peptides are substrates, but with decreased affinity. These studies establish that structural information important for NMT-ligand interaction exists beyond the first two amino acids in peptide substrates and that the side chains of residue 5 play a critical role in the binding of substrates to this enzyme.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-22021,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-2409555,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-2416464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-2578615,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-2984663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-2988939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-2989813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-3006923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-3086867,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-3092218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-3100524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-3456589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-3461461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-3489936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-3517877,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-3526330,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-3917576,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-3944142,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-3964651,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-3972848,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-399329,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-4006909,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-6302307,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-6340098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-6436247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-6595656,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-6959104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-7017716,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3106975-7160476
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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 |
May
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
84
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2708-12
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
1987
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pubmed:articleTitle |
Purification and characterization of yeast myristoyl CoA:protein N-myristoyltransferase.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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