Human adenine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme.

Article Details

Citation

Wilson JM, O'Toole TE, Argos P, Shewach DS, Daddona PE, Kelley WN

Human adenine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme.

J Biol Chem. 1986 Oct 15;261(29):13677-83.

PubMed ID
3531209 [ View in PubMed
]
Abstract

We defined the amino acid sequence of adenine phosphoribosyltransferase isolated from human erythrocytes. Peptide fragments formed by cleavage at arginine, lysine, glutamic acid, and methionine were purified by high pressure liquid chromatography and sequenced by manual Edman degradation. The complete primary structure of human adenine phosphoribosyltransferase was established by sequence analysis of 19 peptide fragments. Presumed homology between the human and rodent enzymes was used to order fragments that had inadequate overlapping sequences. The enzyme has 179 residues with a calculated subunit molecular weight of 19,481. Mass spectrometry indicated that the NH2-terminal residue is acetylated. Human adenine phosphoribosyltransferase has sequence homology with xanthine-guanine phosphoribosyltransferase from Escherichia coli in 110-amino acid region encompassing the NH2-terminal section of the enzyme.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Adenine phosphoribosyltransferaseP07741Details