PMID: 1731867Jan 14, 1992Paper

Serine hydroxymethyltransferase: origin of substrate specificity

Biochemistry
S AngelaccioV Schirch

Abstract

All forms of serine hydroxymethyltransferase, for which a primary structure is known, have five threonine residues near the active-site lysyl residue (K229) that forms the internal aldimine with pyridoxal phosphate. For Escherichia coli serine hydroxymethyltransferase each of these threonine residues has been changed to an alanine residue. The resulting five mutant enzymes were purified and characterized with respect to kinetic and spectral properties. The mutant enzymes T224A and T227A showed no significant changes in kinetic and spectral properties compared to the wild-type enzyme. The T225A and T230A enzymes exhibited differences in Km and kcat values but exhibited the same spectral properties as the wild-type enzyme. The four threonine residues at positions 224, 225, 227, and 230 do not play a critical role in the mechanism of the enzyme. The T226A enzyme had nearly normal affinity for substrates and coenzymes but had only 3% of the catalytic activity of the wild-type enzyme. The spectrum of the T226A enzyme in the presence of amino acid substrates showed a large absorption maximum at 343 nm with only a small absorption band at 425 nm, unlike the wild-type enzyme whose enzyme-substrate complexes absorb at 425 nm. Rapid reac...Continue Reading

Citations

Oct 7, 1998·Protein Science : a Publication of the Protein Society·S PascarellaF Bossa
Sep 23, 2006·Science in China. Series C, Life Sciences·Mingxuan XuGuoping Zhao
Apr 27, 1995·Biochimica Et Biophysica Acta·R A John
Apr 13, 2000·The International Journal of Biochemistry & Cell Biology·N A RaoH S Savithri
Jan 28, 2009·Antimicrobial Agents and Chemotherapy·Yann DurocThierry Meinnel
Jun 2, 2007·Protein Expression and Purification·Sarita Sharma, Vinod Bhakuni
Aug 21, 2013·BioMed Research International·Martino L Di SalvoH Tonie Wright
Dec 17, 2014·Experimental Parasitology·Shashi GandhiJitendra Kumar Saxena
Aug 13, 2003·The Journal of Biological Chemistry·Sarita Chaturvedi, Vinod Bhakuni
Apr 16, 1998·The Journal of Biological Chemistry·G P VatcherD L Baillie
Dec 1, 1993·Microbiological Reviews·M Riley

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