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pubmed-article:8363605pubmed:abstractTextThe role of Cys-138 in the catalysis of the skeletal muscle 6-phosphofructo-2-kinase reaction was investigated by mutating this residue to serine, glutamine and alanine, expressing the mutants in E. coli with a T7 RNA polymerase-based expression system, and analyzing their kinetic properties. The Cys138Ala mutant had greatly diminished activity, while the Cys138Ser and Cys138Gln mutants had maximal velocities 2-3 fold higher than the wild-type enzyme. It was concluded that Cys-138 does not act as a base catalyst in the kinase reaction, but that it plays a significant structural role in the enzyme's active site.lld:pubmed
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pubmed-article:8363605pubmed:articleTitleLack of evidence for a role of Cys-138 as a base catalyst in the skeletal muscle 6-phosphofructo-2-kinase reaction.lld:pubmed
pubmed-article:8363605pubmed:affiliationDepartment of Physiology and Biophysics, State University of New York, Stony Brook 11794-8661.lld:pubmed
pubmed-article:8363605pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8363605pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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