Vorísek J, Rehácek Z
Arch Microbiol. 1978 Jun 26;117(3):297-302. doi: 10.1007/BF00738550.
Acetyl coenzyme A (CoA) carboxylase (EC 6.4.1.2), an enzyme catalyzing the synthesis of malonyl-CoA, was cytochemically localized in endoplasmic reticulum (ER) of sclerotia-like cells of submerged Claviceps purpurea Tul. producing clavine alkaloids. The enzymic activity was structurally bound in unit membranes of ER strands which, later on, evolved into vacuoles containing lipoprotein material. The reaction product was absent from ER in nonvacuolized filamentous hyphae and ovoid asexual spores containing numerous lipid globules; it was also absent from ER in the mycelium of submerged C. purpurea strain producing no alkaloids. In view of our previous morphogenetic observations and the available biochemical evidence, the observed localization of acetyl-CoA carboxylase was assumed not to coincide with fatty acid biosynthesis but to represent sites of alkaloid synthesis.
乙酰辅酶A（CoA）羧化酶（EC 6.4.1.2）是一种催化丙二酰辅酶A合成的酶，通过细胞化学方法定位在深层紫麦角菌（Claviceps purpurea Tul.）产生棒麦角碱的菌核状细胞的内质网（ER）中。酶活性在ER链的单位膜中结构上结合，随后这些膜演变成含有脂蛋白物质的液泡。在未液泡化的丝状菌丝和含有大量脂质球的卵形无性孢子的ER中没有反应产物；在不产生生物碱的深层紫麦角菌菌株的菌丝体的ER中也没有反应产物。鉴于我们之前的形态发生观察和现有的生化证据，推测观察到的乙酰辅酶A羧化酶的定位与脂肪酸生物合成不一致，而是代表生物碱合成的位点。
