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本文引用的文献

1

Degradation of chloroaromatics: purification and characterization of maleylacetate reductase from Pseudomonas sp. strain B13.氯代芳烃的降解：来自假单胞菌属B13菌株的马来酰乙酸还原酶的纯化与表征

J Bacteriol. 1993 Oct;175(19):6075-81. doi: 10.1128/jb.175.19.6075-6081.1993.

2

Purification and characterization of maleylacetate reductase from Alcaligenes eutrophus JMP134(pJP4).从嗜碱假单胞菌JMP134(pJP4)中纯化和鉴定马来酸乙酸还原酶

J Bacteriol. 1993 Nov;175(21):6745-54. doi: 10.1128/jb.175.21.6745-6754.1993.

3

Maleylacetate reductase of Pseudomonas sp. strain B13: specificity of substrate conversion and halide elimination.假单胞菌属B13菌株的马来酰乙酸还原酶：底物转化特异性和卤化物消除

J Bacteriol. 1995 Jan;177(2):320-5. doi: 10.1128/jb.177.2.320-325.1995.

4

Hybrid pathway for chlorobenzoate metabolism in Pseudomonas sp. B13 derivatives.假单胞菌属B13衍生物中氯苯甲酸代谢的混合途径。

J Bacteriol. 1980 May;142(2):467-73. doi: 10.1128/jb.142.2.467-473.1980.

5

Isolation and characterization of a 3-chlorobenzoate degrading pseudomonad.一株降解3-氯苯甲酸假单胞菌的分离与鉴定

Arch Microbiol. 1974;99(1):61-70. doi: 10.1007/BF00696222.

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Degradation of 1,2-dichlorobenzene by a Pseudomonas sp.一株假单胞菌对1,2-二氯苯的降解作用

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7

Sequence analysis of the Pseudomonas sp. strain P51 tcb gene cluster, which encodes metabolism of chlorinated catechols: evidence for specialization of catechol 1,2-dioxygenases for chlorinated substrates.编码氯代儿茶酚代谢的假单胞菌属菌株P51的tcb基因簇的序列分析：儿茶酚1,2-双加氧酶对氯代底物特异性的证据

J Bacteriol. 1991 Apr;173(8):2425-34. doi: 10.1128/jb.173.8.2425-2434.1991.

8

Characterization of isofunctional ring-cleaving enzymes in aniline and 3-chloroaniline degradation by Pseudomonas acidovorans CA28.嗜酸假单胞菌CA28对苯胺和3-氯苯胺降解过程中同功环裂解酶的特性研究

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9

Chemical structure and biodegradability of halogenated aromatic compounds. Substituent effects on 1,2-dioxygenation of catechol.卤代芳香化合物的化学结构与生物降解性。取代基对儿茶酚1,2-双加氧作用的影响。

Biochem J. 1978 Jul 15;174(1):85-94. doi: 10.1042/bj1740085.

利用改良邻位途径的氯代芳烃降解细菌中的马来酰乙酸还原酶：催化特性比较

Maleylacetate reductases in chloroaromatic-degrading bacteria using the modified ortho pathway: comparison of catalytic properties.

作者信息

Müller D, Schlömann M, Reineke W

机构信息

Bergische Universität-Gesamthochschule Wuppertal, Germany.

出版信息

J Bacteriol. 1996 Jan;178(1):298-300. doi: 10.1128/jb.178.1.298-300.1996.

DOI:10.1128/jb.178.1.298-300.1996

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC177654/

Abstract

The maleylacetate reductases from Pseudomonas aeruginosa RHO1 and Alcaligenes eutrophus JMP134 were tested for activity and affinity to various maleylacetates as well as dechlorinating properties. The dechlorinating activity and the kcat/Km values revealed high-level similarity of these reductases to that of Pseudomonas sp. strain B13.

摘要

对铜绿假单胞菌RHO1和食碱假单胞菌JMP134中的马来酸乙酸还原酶进行了测试，以考察其对各种马来酸乙酸的活性、亲和力以及脱氯特性。脱氯活性和催化常数与米氏常数的比值显示，这些还原酶与假单胞菌属菌株B13的还原酶具有高度相似性。