The primary structure of human H-protein of the glycine cleavage system deduced by cDNA cloning

Biochem Biophys Res Commun. 1991 Apr 30;176(2):711-6. doi: 10.1016/s0006-291x(05)80242-6.

Abstract

A full-length cDNA encoding the human H-protein of the glycine cleavage system has been isolated from a lambda gt11 human fetal liver cDNA library. The cDNA insert was 1091 base pairs with an open reading frame of 519 base pairs which encoded a 125-amino acid mature human H-protein with a 48-amino acid presequence. Human H-protein is 97%, 86%, and 46% identical to the bovine, chicken, and pea H-protein, respectively.

MeSH terms

  • Amino Acid Oxidoreductases*
  • Amino Acid Sequence
  • Animals
  • Base Composition
  • Base Sequence
  • Carrier Proteins / biosynthesis
  • Carrier Proteins / genetics*
  • Cattle
  • Chickens
  • Cloning, Molecular
  • DNA / chemistry*
  • Fabaceae / genetics
  • Genomic Library
  • Glycine / metabolism
  • Glycine Decarboxylase Complex H-Protein
  • Glycine Dehydrogenase (Decarboxylating)
  • Humans
  • Hydrolysis
  • Liver / chemistry*
  • Molecular Sequence Data
  • Plants, Medicinal
  • Restriction Mapping
  • Sequence Homology, Nucleic Acid

Substances

  • Carrier Proteins
  • Glycine Decarboxylase Complex H-Protein
  • DNA
  • Amino Acid Oxidoreductases
  • Glycine Dehydrogenase (Decarboxylating)
  • Glycine

Associated data

  • GENBANK/D90312
  • GENBANK/D90313
  • GENBANK/M62480
  • GENBANK/M62481
  • GENBANK/M62482
  • GENBANK/M69175
  • GENBANK/M69176
  • GENBANK/M69194
  • GENBANK/M72238
  • GENBANK/X53944