Williamson J M, Meyer R, Inamine E
Antimicrob Agents Chemother. 1985 Oct;28(4):478-84. doi: 10.1128/AAC.28.4.478.
Cystathionine gamma-lyase (EC 4.4.1.1) was purified from Streptomyces cattleya, an actinomycete which produces the unusual beta-lactam antibiotic thienamycin. The enzyme displays broad substrate specificity and is similar to gamma-lyases purified from other microorganisms. That the gamma-lyase functions in vivo to provide cysteine for antibiotic synthesis was shown by two types of experiments. First, cystathionine and methionine, as well as cysteine itself, are efficiently utilized by S. cattleya for thienamycin biosynthesis. Second, propargylglycine, a mechanism-based inactivator of cystathionine gamma-lyase in vitro, inhibits the synthesis of thienamycin in vivo. This inhibition can be substantially reversed by providing the cells with another source of cysteine, such as cystine.
胱硫醚γ-裂合酶(EC 4.4.1.1)是从产黄青霉中纯化得到的,产黄青霉是一种放线菌,可产生不寻常的β-内酰胺抗生素硫霉素。该酶具有广泛的底物特异性,与从其他微生物中纯化得到的γ-裂合酶相似。通过两种实验表明,γ-裂合酶在体内发挥作用,为抗生素合成提供半胱氨酸。首先,产黄青霉能有效利用胱硫醚、蛋氨酸以及半胱氨酸本身进行硫霉素生物合成。其次,炔丙基甘氨酸是胱硫醚γ-裂合酶在体外的基于机制的失活剂,它能在体内抑制硫霉素的合成。通过为细胞提供另一种半胱氨酸来源,如胱氨酸,这种抑制作用可得到显著逆转。