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Cloning and molecular characterization of a presumptive argF , a structural gene encoding ornithine carbamoyl transferase (OCT), in the cyanobacterium Nostoc sp. PCC 73102
Author(s) -
Jansson Eva,
Lindblad Peter
Publication year - 1998
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1034/j.1399-3054.1998.1030307.x
Subject(s) - ornithine , biology , peptide sequence , biochemistry , amino acid , ornithine carbamoyltransferase , transferase , gene , molecular cloning , terminator (solar) , nostoc , microbiology and biotechnology , ornithine aminotransferase , structural gene , nucleic acid sequence , genetics , enzyme , cyanobacteria , arginine , escherichia coli , bacteria , ionosphere , physics , astronomy
Ornithine carbamoyl transferase (OCT), encoded by argF , catalyzes the formation of citrulline from ornithine and carbamoyl phosphate. A presumptive argF from the filamentous cyanobacterium Nostoc sp. PCC 73102 has been cloned and sequenced. A transcriptional terminator sequence is suggested downstream of the structural gene. Amino acids known to be involved in binding the substrate carbamoyl phosphate and ornithine were observed within the sequence. The deduced amino acid sequence showed 69% identity to the deduced amino acid sequence from Synechocystis sp. PCC 6803, but less identities (30‐46@) to OCTs from other organisms. The subunits of the deduced protein had a calculated molecular mass of 33 368 Da. Northern blot experiments demonstrated a single transcript with an approximate size of 0.95 kb.