rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
25
|
pubmed:dateCreated |
1985-4-18
|
pubmed:abstractText |
The bifunctional enzyme involved in tyrosine biosynthesis, chorismate mutase/prephenate dehydrogenase, has been isolated from extracts of a regulatory mutant of Escherichia coli K12. The pure enzyme is a homodimer of total molecular weight 78 000 and displays Michaelis-Menten kinetics for both activities. Fingerprinting and amino acid sequencing of tryptic and thermolytic peptides of the S-[14C]carboxymethylated enzyme allowed the identification of three unique cysteine-containing sequences per subunit. Chemical modification of the native enzyme with 5,5'-dithiobis(2-nitrobenzoate) or iodoacetamide showed that one sulfhydryl group per subunit was particularly reactive, and the integrity of this group was essential for both enzymic activities. This work supports previous proposals for a close spatial relationship between the active sites.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0006-2960
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
4
|
pubmed:volume |
23
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
6240-9
|
pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:6395895-Amino Acid Sequence,
pubmed-meshheading:6395895-Centrifugation,
pubmed-meshheading:6395895-Chemical Phenomena,
pubmed-meshheading:6395895-Chemistry,
pubmed-meshheading:6395895-Chorismate Mutase,
pubmed-meshheading:6395895-Chromatography, Affinity,
pubmed-meshheading:6395895-Cysteine,
pubmed-meshheading:6395895-Dithionitrobenzoic Acid,
pubmed-meshheading:6395895-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6395895-Escherichia coli,
pubmed-meshheading:6395895-Iodoacetamide,
pubmed-meshheading:6395895-Isomerases,
pubmed-meshheading:6395895-Kinetics,
pubmed-meshheading:6395895-Molecular Weight,
pubmed-meshheading:6395895-Oxidoreductases,
pubmed-meshheading:6395895-Peptide Fragments,
pubmed-meshheading:6395895-Prephenate Dehydrogenase,
pubmed-meshheading:6395895-Thermolysin,
pubmed-meshheading:6395895-Trypsin
|
pubmed:year |
1984
|
pubmed:articleTitle |
Chorismate mutase/prephenate dehydrogenase from Escherichia coli K12: purification, characterization, and identification of a reactive cysteine.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|