Abstract

The complete amino acid sequence of cytosolic serine hydroxymethyltransferase from rabbit liver was determined. The sequence was determined from analysis of peptides isolated from tryptic and cyanogen bromide cleavages of the enzyme. Special procedures were used to isolate and sequence the C-terminal and blocked N-terminal peptides. Each of the four identical subunits of the enzyme consists of 483 residues. The sequence could be easily aligned with the sequence of Escherichia coli serine hydroxymethyltransferase. The primary structural homology between the rabbit and E. coli enzymes is about 42%. The importance of the primary and predicted secondary structural homology between the two enzymes is discussed.

Highlights

  • The complete amino acid sequence of cytosolic serine hydroxymethyltransferase from rabbit liver was determined

  • The sequence could be aligned with the sequence of Escherichia coli serine hydroxymethyltransferase.The primary structural homology between the rabbit and E. coli enzymes is about 42%.The importance of the primary and predicted secondary structural homology between the two enzymes is discussed

  • In this paper we report the complete amino acid sequence of rabbit liver cytosolic serine hydroxymethyltransferase which has been determined by classical protein sequencing methods

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Summary

DISCUSSION

The amino acid sequence of rabbit liver cytosolic serine hydroxymethyltransferase is compared in Fig. 2 with that of the protein codedby the glyA gene of E. coli, whichwas identified as the bacterial version of this enzyme [10]. We have recently changed an active site histidine to an asparagine in the E. coli enzyme [2] The importance of this histidine was suggestedby the conservation of an 11-residue amino acid sequence between the rabbit cytosolic and mitochondrial isozymes and theE. We are currently sequencing these cDNA clones to see whether they code for cytosolic serine hydroxymethyltransferase

EXPERIMENTAL PROCEDURES
RESULTS
KG T O GG R
91 Ilk 2 - I l e 71
LZa 4-12
Findings
93 IPhe 3-Phe 91
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