PMID:1802033
| Citation |
Stauffer, LT, Steiert, PS, Steiert, JG and Stauffer, GV (1991) An Escherichia coli protein with homology to the H-protein of the glycine cleavage enzyme complex from pea and chicken liver. DNA Seq. 2:13-7 |
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| Abstract |
The nucleotide sequence of an Escherichia coli gene which presumably encodes the H-protein of the glycine cleavage (GCV) enzyme complex is presented. The gene, designated gcvH, encodes a polypeptide of 128 amino acids with a calculated molecular weight of 13,665 daltons. The translation start site was determined by N-terminal amino acid sequence analysis of a gcvH-lacZ encoded fusion protein. The E. coli H-protein shows extensive homology with the H-proteins from the pea (Pisum sativum) and the chicken liver GCV enzyme complexes. 85 of 128 amino acid residues are identical or chemically similar between the E. coli and the pea H-proteins, and 74 of 128 amino acid residues are identical or chemically similar between the E. coli and the chicken liver H-proteins. All three proteins have identical amino acid sequences from residues 61-65. This sequence contains the lysyl residue involved in lipoic acid attachment in the chicken liver H-protein. |
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| Keywords |
Amino Acid Oxidoreductases; Amino Acid Sequence; Animals; Bacterial Proteins/genetics; Base Sequence; Carrier Proteins/genetics; Chickens; DNA, Bacterial/genetics; Escherichia coli/genetics; Fabaceae; Genes, Bacterial; Glycine Decarboxylase Complex H-Protein; Glycine Dehydrogenase (Decarboxylating); Liver; Molecular Sequence Data; Plants, Medicinal; Protein Biosynthesis; Sequence Homology, Nucleic Acid |
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This paper determines the sequence of the gcvH product and shows that it has sequence similarity to the chicken liver and pea.
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