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Sequence homology between prokaryotic and eukaryotic forms of serine hydroxymethyltransferase.

Abstract：

:The sequence of tryptic and chymotryptic peptides from cytosolic and mitochondrial rabbit liver serine hydroxymethyltransferase are compared to the proposed sequence of a protein coded for by the glyA gene of Escherichia coli. The E. coli glyA gene is believed to code for serine hydroxymethyltransferase. Extensive sequence homology between these peptides were found for the proposed E. coli enzyme in the aminoterminal two-thirds of the molecule. All three proteins have identical sequences from residue 222-231. This sequence is known to contain the lysyl residue which forms a Schiff's base with pyridoxal-P in the two rabbit liver enzymes. These results support the interpretation that the proposed sequence of E. coli serine hydroxymethyltransferase is correct. The data also show that cytosolic and mitochondrial serine hydroxymethyltransferase are homologous proteins.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Barra D,Martini F,Angelaccio S,Bossa F,Gavilanes F,Peterson D,Bullis B,Schirch L

doi

10.1016/s0006-291x(83)80242-3

subject

Has Abstract

pub_date

1983-11-15 00:00:00

pages

1007-12

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)80242-3

journal_volume

116

pub_type

杂志文章

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