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Formation of 5,5-dimethyl-delta2-thiazoline-4-carboxylic acid during cleavage of penicillin G by D-alanine carboxypeptidase from Bacillus stearothermophilus.

作者信息

Hammarström S, Strominger J L

出版信息

J Biol Chem. 1976 Dec 25;251(24):7947-9.

PMID:1002716
Abstract
摘要

相似文献

1
Formation of 5,5-dimethyl-delta2-thiazoline-4-carboxylic acid during cleavage of penicillin G by D-alanine carboxypeptidase from Bacillus stearothermophilus.
J Biol Chem. 1976 Dec 25;251(24):7947-9.
2
Degradation of penicillin G to phenylacetylglycine by D-alanine carboxypeptidase from Bacillus stearothermophilus.嗜热脂肪芽孢杆菌的D-丙氨酸羧肽酶将青霉素G降解为苯乙酰甘氨酸。
Proc Natl Acad Sci U S A. 1975 Sep;72(9):3463-7. doi: 10.1073/pnas.72.9.3463.
3
Stability of D-5,5-dimethyl-delta2-thiazoline-4-carboxylic acid in relation to its possible occurrence as a degradation product of penicillin by the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and the membrane-bound dd-carboxypeptidase from Bacillus stearothermophilus.D-5,5-二甲基-δ2-噻唑啉-4-羧酸的稳定性,这涉及到它作为青霉素降解产物可能的产生情况,该降解由来自链霉菌R61的胞外DD-羧肽酶-转肽酶以及来自嗜热脂肪芽孢杆菌的膜结合dd-羧肽酶引发。
J Biol Chem. 1978 May 25;253(10):3660-5.
4
Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases.青霉素作用机制:青霉素和底物在两种细菌D-丙氨酸羧肽酶中与同一个活性位点丝氨酸共价结合。
Proc Natl Acad Sci U S A. 1979 Jun;76(6):2730-4. doi: 10.1073/pnas.76.6.2730.
5
The mechanism of action of penicillin. Penicillin acylates the active site of Bacillus stearothermophilus D-alanine carboxypeptidase.青霉素的作用机制。青霉素使嗜热脂肪芽孢杆菌D - 丙氨酸羧肽酶的活性位点发生酰化。
J Biol Chem. 1980 May 10;255(9):3977-86.
6
Limited proteolysis of the penicillin-sensitive D-alanine carboxypeptidase purified from Bacillus subtilis membranes. Active water-soluble fragments generated by cleavage of a COOH-terminal membrane anchor.对从枯草芽孢杆菌膜中纯化的青霉素敏感的D-丙氨酸羧肽酶进行有限的蛋白酶解。通过切割COOH末端膜锚产生活性水溶性片段。
J Biol Chem. 1981 Feb 25;256(4):2059-66.
7
Primary structure of the COOH-terminal membranous segment of a penicillin-sensitive enzyme purified from two Bacilli.从两种芽孢杆菌中纯化得到的一种青霉素敏感酶的COOH末端膜状片段的一级结构。
J Biol Chem. 1981 Feb 25;256(4):2067-77.
8
Kinetic evidence for an acyl-enzyme intermediate in D-alanine carboxypeptidases of Bacillus subtilis and Bacillus stearothermophilus.枯草芽孢杆菌和嗜热脂肪芽孢杆菌D-丙氨酸羧肽酶中酰基酶中间体的动力学证据。
J Biol Chem. 1977 May 10;252(9):2934-9.
9
Binding of (14C)penicillin G to the membrane-bound and the purified D-alanine carboxypeptidases from Bacillus stearothermophilus and Bacillus subtilis and its release.(14C)青霉素G与嗜热脂肪芽孢杆菌和枯草芽孢杆菌的膜结合型及纯化的D-丙氨酸羧肽酶的结合及其释放
J Biol Chem. 1974 Nov 10;249(21):6828-35.
10
Purification and characterization of the thermophilic D-alanine carboxypeptidase from membranes of Bacillus stearothermophilus.嗜热脂肪芽孢杆菌膜中嗜热D-丙氨酸羧肽酶的纯化与特性分析
J Biol Chem. 1974 Aug 10;249(15):4863-71.

引用本文的文献

1
A point mutation leads to altered product specificity in beta-lactamase catalysis.一个点突变导致β-内酰胺酶催化中产物特异性的改变。
Proc Natl Acad Sci U S A. 1997 Jan 21;94(2):443-7. doi: 10.1073/pnas.94.2.443.
2
Simultaneous release of penicilloic acid and phenylacetyl glycine by penicillin-binding proteins 5 and 6 of Escherichia coli.大肠杆菌青霉素结合蛋白5和6同时释放青霉噻唑酸和苯乙酰甘氨酸。
J Bacteriol. 1984 Nov;160(2):822-3. doi: 10.1128/jb.160.2.822-823.1984.
3
Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis.
从枯草芽孢杆菌的D-丙氨酸羧肽酶中分离青霉素结合肽。
Proc Natl Acad Sci U S A. 1977 Mar;74(3):1009-12. doi: 10.1073/pnas.74.3.1009.