transamidination

English Journal

Crystal structure of L-arginine:inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus: an enzyme involved in streptomycin biosynthesis.

Fritsche E, Bergner A, Humm A, Piepersberg W, Huber R.SourceMax-Planck-Institut für Biochemie, Abteilung für Strukturforschung, Martinsried, Germany.
Biochemistry.Biochemistry.1998 Dec 22;37(51):17664-72.
Inosamine-phosphate amidinotransferases catalyze two nonconsecutive transamidination reactions in the biosynthesis of the streptomycin family of antibiotics. L-Arginine:inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus (StrB1) was cloned as an N-terminal hexa-histidine fusion pr
PMID 9922132

Humm A, Fritsche E, Steinbacher S.SourceMax-Planck-Institut für Biochemie, Abt. Strukturforschung, Martinsried, Germany.
Biological chemistry.Biol Chem.1997 Mar-Apr;378(3-4):193-7.
L-Arginine:glycine amidinotransferase (AT) catalyzes the committed step in creatine biosynthesis by formation of guanidinoacetic acid, the direct precursor of creatine. The X-ray structure of the human enzyme shows a novel fold with fivefold pseudosymmetry of beta beta alphabeta-modules. These modul
PMID 9165070

Synthesis of neuroactive guanidino compounds by rat kidney L-arginine: glycine amidinotransferase.

Watanabe Y, Van Pilsum JF, Yokoi I, Mori A.SourceDepartment of Neuroscience, Okayama University Medical School, Japan.
Life sciences.Life Sci.1994;55(5):351-8.
Several neuroactive guanidino compounds have been reported to be synthesized in mammals by transamidination reactions. The enzyme(s) responsible for their synthesis and their location in the body has not been well established. The purpose of this investigation was to determine if purified homogeneou
PMID 8035648