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Arginine metabolism in chlamydomonas reinhardi . A new type of citrulline degradation
Author(s) -
Sussenbach J.S.,
Strijkert P.J.
Publication year - 1970
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(70)80179-x
Subject(s) - chlamydomonas , citation , library science , arginine , chemistry , computer science , biochemistry , amino acid , mutant , gene
The study of the regulation of the arginine biosynthesis in Chlumydomonas [ 1, 21 is complicated by the degradation of arginine. As we reported earlier [3], the first enzyme of the catabolic pathway is arginine deiminase (L-arginine imino hydrolase, EC 3.5.3.6.). This enzyme causes the breakdown of arginine to citrulline and ammonia. Citrulline is then further degraded. Two pathways for the degradation of citrulline have been reported. This communication describes a third hitherto unknown route in Chlamydomonas. The enzyme involved in the reaction exhibits a pH optimum of 8.5, needs no cofactors, and is inhibited by orthophosphate. Formation of ornithine and ammonia are not observed, thus excluding the possibility that this enzyme is identical with citrulline hydrolase. Thin-layer chromatography of radioactive reaction products shows the formation of a product, lacking intact ureido and a-amino groups, but still containing all the carbon atoms of citrulline.