Hammarström S, Strominger J L
Proc Natl Acad Sci U S A. 1975 Sep;72(9):3463-7. doi: 10.1073/pnas.72.9.3463.
D-Alanine carboxypeptidase from Bacillus stearothermophilus is a membrane-bound enzyme which is inhibited by covalent interaction with penicillin G. The penicilloyl enzyme spontaneously reactivates and simultaneously releases a penicillin G degradation product; 0.2 mumol of the latter was isolated after incubation of 4.2 mumol of [8-14C]penicillin G with 10 g of membrane protein. It was identified as phenylacetylglycine by chromatographic techniques, infrared spectroscopy, and mass spectrometry. A mechanism for the degradation is proposed in which the remaining part of penicillin G would be released as 5,5-dimethyl-delta2-thiazoline-4-carboxylic acid. The implications of this finding are discussed.
嗜热脂肪芽孢杆菌的D-丙氨酸羧肽酶是一种膜结合酶，可通过与青霉素G的共价相互作用而被抑制。青霉素酰化酶会自发重新激活，同时释放出一种青霉素G降解产物；用4.2 μmol的[8-¹⁴C]青霉素G与10 g膜蛋白孵育后，分离出了0.2 μmol的后者。通过色谱技术、红外光谱和质谱鉴定其为苯乙酰甘氨酸。提出了一种降解机制，其中青霉素G的其余部分将以5,5-二甲基-δ²-噻唑啉-4-羧酸的形式释放。讨论了这一发现的意义。
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