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Abstract

  1. Top of page
  2. Abstract
  3. REFERENCES

The amino acid sequence of glutamate decarboxylase from Escherichia coli was solved by a combination of automated Edman degradation of peptide fragments derived by proteolytic and chemical cleavage and sequencing of DNA. Correct alignment of three peptides, for which no peptide overlaps were available, was achieved by sequencing a 1.1-kbp fragment of DNA produced by a polymerase-chain reaction using primers corresponding to sequences known to be in amino-terminal and carboxy-terminal regions of the protein. Sequence similarity (24% identity) with mammalian glutamate decarboxylase was found to be limited to a 55-residue sequence around the lysine residue that with binds the coenzyme. Stronger similarity (38% identity), again confined to the same region, is seen with bacterial pyridoxal-phosphate-dependent histidine decarboxylase.

Abbreviations
Pyridoxal P

pyridoxal phosphate

PCR

polymerase-chain reaction

Enzymes
 

Glutamate decarboxylase (EC 4.1.1.15)

 

histidine decarboxylase (EC 4.1.1.22)

 

trypsin (EC 3.4.21.4)

 

Staphylococcal V8 protease (EC 3.4.21.19)

 

pepsin (EC 3.4.23.1)

Dedication
 

This paper is dedicated to Prof. A. Ballio on the occasion of his 70th birthday

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