Serine Transhydroxymethylase
نویسندگان
چکیده
منابع مشابه
Serine transhydroxymethylase isoenzymes from a facultative methylotroph.
Two serine transhydroxymethylase activities have been purified from a facultative methylotrophic bacterium. One enzyme predominates when the organism is grown on methane or methanol as the sole carbon and energy source, whereas the second enzyme is the major isoenzyme found when succinate is used as the sole carbon and energy source. The enzyme from methanol-grown cells is activated by glyoxyla...
متن کاملRegulation of serine transhydroxymethylase activity in Salmonella typhimurium.
The regulation of serine transhydroxymethylase (EC 2.1.2.1.; l-serine:tetrahydrofolic-5,10-hydroxymethyltransferase) has been investigated in Salmonella typhimurium LT2. Our results indicate that limitation of a methionine auxotroph for methionine does not cause derepression of this enzyme as reported for Escherichia coli. However, a sixfold decrease in specific activity was observed when S. ty...
متن کاملSerine transhydroxymethylase. Studies on the role of tetrahydrofolate.
Studies of the reversible interconversion of glycine and serine catalyzed by rabbit liver serine transhydroxymethylase in the presence and in the absence of tetrahydrofolate are described. The studies include measurements of pHrate profiles, isotope effects, and spectral properties of the enzyme-substrate complexes. Vma, values for the synthesis of serine from glycine and formaldehyde and the e...
متن کاملSelection of Salmonella typhimurium mutants with altered serine transhydroxymethylase regulation.
In Salmonella typhimurium the glyA gene product, serine transhydroxymethylase (E.C. 2.1.2.1.; L-serine:tetrahydrofolate-5,10-hydroxymethyltransferase) is responsible for the interconversion of serine and glycine. This reaction also provides the cell with one-carbon units from the 5,10-methylene-tetrahydrofolate formed during glycine synthesis. Despite the importance of this enzyme, however, no ...
متن کاملEvidence for the involvement of serine transhydroxymethylase in serine and glycine interconversions in Salmonella typhimurium.
Salmonella typhimurium can normally use glycine as a serine source to support the growth of serine auxotrophs. This reaction was presumed to occur by the reversible activity of the enzyme, serine transhydroxymethylase (E. C. 2. 1. 2. 1; L-serine: tetrahydrofolic-5, 10 transhydroxymethylase), which is responsible for glycine biosynthesis. However, this enzyme had not been demonstrated to be sole...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)43182-7