1992
DOI: 10.1016/s0021-9258(19)37096-6
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Escherichia coli serine hydroxymethyltransferase. The role of histidine 228 in determining reaction specificity.

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Cited by 42 publications
(11 citation statements)
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“…In the absence of an X-ray crystal structure, past studies have been performed by chemical modification and site-directed mutagenesis based on amino acid residues that are totally conserved across the known SHMT protein sequences. Much of this work has concentrated on the dimeric enzyme from Escherichia coli [18][19][20][21][22] and on the tetrameric sheep liver enzyme [23,24].…”
Section: Figurementioning
confidence: 99%
“…In the absence of an X-ray crystal structure, past studies have been performed by chemical modification and site-directed mutagenesis based on amino acid residues that are totally conserved across the known SHMT protein sequences. Much of this work has concentrated on the dimeric enzyme from Escherichia coli [18][19][20][21][22] and on the tetrameric sheep liver enzyme [23,24].…”
Section: Figurementioning
confidence: 99%
“…The glycine-dependent aldolases are pyridoxal 5-phosphate-dependent enzymes which catalyze the reversible aldol reaction of glycine with an aldehyde acceptor to form a β-hydroxy-α-amino acid …”
Section: Glycine-dependent Aldolasesmentioning
confidence: 99%
“…In vivo SHMT (EC 2.1.2.1) catalyzes the reversible aldol reaction between glycine and formaldehyde to give l -serine. For this reaction the cofactor tetrahydrofolate (THF) is required, which binds nonenzymatically with formaldehyde to form N 5 , N 10 -methylenetetrahydrofolate which is then accepted by the enzyme 125a…”
Section: Glycine-dependent Aldolasesmentioning
confidence: 99%
“…There are few well-characterized examples of hydroxymethyltransferases, with serine hydroxymethyltransferase being the most thoroughly studied ( ). This enzyme contains PLP and, after transimination with l -serine, catalyzes the cleavage of the Cα−Cβ bond to generate formaldehyde and glycine.…”
mentioning
confidence: 99%