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The amino acid sequences of human and pig l ‐arginine:glycine amidinotransferase
Author(s) -
Humm Andreas,
Huber Robert,
Mann Karlheinz
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80394-3
Subject(s) - amino acid , biochemistry , biology , glycine , proteolysis , arginine , peptide sequence , complementary dna , enzyme , gene
We have isolated and sequenced the l ‐arginine:glycine amidinotransferase of pig kidney mitochondria. Due to endogenous proteolysis, the purified molecules showed some heterogeneity at the N terminus. The longest form recovered had 386 amino acids. Part of the pig amidinotransferase sequence information was used to isolate cDNA clones coding for the human enzyme. The deduced amino acid of the human amidinotransferase was 37 amino acids longer due to the presence of a signal sequence. The mature proteins were 94% identical to each other and 36% identical to the sequences of bacterial l ‐argininednosamine phosphate amidinotransferases.