Lim D V, Qadri S M, Williams R P
Appl Environ Microbiol. 1976 May;31(5):738-42. doi: 10.1128/aem.31.5.738-742.1976.
A Put mutant of Serratia marcescens, deficient in proline oxidase and therefore unable to degrade proline, was used to assay for an enzymatic reaction responsible for incorporation of proline into prodigiosin. The reaction had a pH optimum of 7.5 and a Km of 1.1 X 10(-4) M at 27 C. At temperatures above 27 C, the velocity of the reaction decreased with increasing temperature and little activity was detected at 42 C. Activity of the enzyme was directly proportional to the quantity of pigment formed and was inhibited by thioproline, a substrate analog. These data suggested the presence of a unique and specific enzyme in the biosynthetic pathway for prodigiosin.
粘质沙雷氏菌的脯氨酸氧化酶缺陷型Put突变体,因其缺乏脯氨酸氧化酶而无法降解脯氨酸,被用于检测将脯氨酸掺入灵菌红素的酶促反应。该反应的最适pH为7.5,在27℃时的米氏常数为1.1×10⁻⁴M。在高于27℃的温度下,反应速度随温度升高而降低,在42℃时几乎检测不到活性。该酶的活性与形成的色素量成正比,并受到底物类似物硫代脯氨酸的抑制。这些数据表明在灵菌红素的生物合成途径中存在一种独特且特异的酶。