Bera T
Mol Biochem Parasitol. 1987 Apr;23(3):183-92. doi: 10.1016/0166-6851(87)90025-9.
L-Arginine stimulates the respiration of Leishmania donovani to rates comparable to those observed with D-glucose. gamma-Guanidinobutyramide, CO2, urea and succinate have been identified as products of L-arginine catabolism by the cell-free extract. The reactions involved in CO2 and urea formation require aerobic conditions. An enzymatic reaction that converts radiolabelled L-arginine to gamma-guanidinobutyramide occurs in cell-free extracts. The enzyme catalyzes a reaction in which O2 consumption and CO2 production are equimolar. The O2 uptake and CO2 production are stimulated by Mg2+, Mn2+, FMN, pyridoxal phosphate, and inhibited by hydroxylamine and NaBH4. L-Arginine decarboxyoxidase is suggested as the trivial name for this enzyme. The enzyme has maximum activity at pH 6.7, and its Km for L-arginine is 3.8 mM. L-Arginine decarboxyoxidase initiates the catabolism of L-arginine (pH less than or equal to 7) in this species, and is followed by the other enzymes of gamma-guanidinobutyramide pathway. Assay procedures have been devised to assay the multiple enzymes of this pathway.
L-精氨酸可刺激杜氏利什曼原虫的呼吸速率，使其与用D-葡萄糖时观察到的速率相当。γ-胍基丁酰胺、二氧化碳、尿素和琥珀酸盐已被鉴定为无细胞提取物中L-精氨酸分解代谢的产物。二氧化碳和尿素形成过程中涉及的反应需要有氧条件。在无细胞提取物中发生了将放射性标记的L-精氨酸转化为γ-胍基丁酰胺的酶促反应。该酶催化的反应中，氧气消耗和二氧化碳产生是等摩尔的。氧气摄取和二氧化碳产生受到镁离子、锰离子、黄素单核苷酸、磷酸吡哆醛的刺激，并受到羟胺和硼氢化钠的抑制。建议将L-精氨酸脱羧氧化酶作为该酶的俗名。该酶在pH 6.7时具有最大活性，其对L-精氨酸的米氏常数为3.8 mM。L-精氨酸脱羧氧化酶启动了该物种中L-精氨酸（pH小于或等于7）的分解代谢，随后是γ-胍基丁酰胺途径的其他酶。已经设计了测定该途径多种酶的测定方法。
