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吡咯喹啉醌的9-羧基是一种新型辅基,在D-葡萄糖脱氢酶全酶的形成中至关重要。

The 9-carboxyl group of pyrroloquinoline quinone, a novel prosthetic group, is essential in the formation of holoenzyme of D-glucose dehydrogenase.

作者信息

Shinagawa E, Matsushita K, Nonobe M, Adachi O, Ameyama M, Ohshiro Y, Itoh S, Kitamura Y

出版信息

Biochem Biophys Res Commun. 1986 Sep 30;139(3):1279-84. doi: 10.1016/s0006-291x(86)80316-3.

DOI:10.1016/s0006-291x(86)80316-3
PMID:3768003
Abstract

Availability of different analogues of pyrroloquinoline quinone as the prosthetic group for apo-D-glucose dehydrogenase was examined. The 9-carboxyl group of pyrroloquinoline quinone was shown to be essential for the reconstitution of the enzyme activity. Although the carboxyl group may not be involved in catalytic function, it is quite probable to contribute the binding of the prosthetic group to apoenzyme.

摘要

研究了不同的吡咯喹啉醌类似物作为脱辅基-D-葡萄糖脱氢酶辅基的可用性。结果表明,吡咯喹啉醌的9-羧基对于酶活性的重建至关重要。虽然羧基可能不参与催化功能,但它很可能有助于辅基与脱辅基酶的结合。

相似文献

1
The 9-carboxyl group of pyrroloquinoline quinone, a novel prosthetic group, is essential in the formation of holoenzyme of D-glucose dehydrogenase.吡咯喹啉醌的9-羧基是一种新型辅基,在D-葡萄糖脱氢酶全酶的形成中至关重要。
Biochem Biophys Res Commun. 1986 Sep 30;139(3):1279-84. doi: 10.1016/s0006-291x(86)80316-3.
2
Enzymatic determination of pyrroloquinoline quinone using crude membranes from Escherichia coli.
Anal Biochem. 1987 Aug 1;164(2):418-23. doi: 10.1016/0003-2697(87)90513-6.
3
Method of enzymatic determination of pyrroloquinoline quinone.吡咯喹啉醌的酶促测定方法。
Anal Biochem. 1985 Dec;151(2):263-7. doi: 10.1016/0003-2697(85)90174-5.
4
Crystal Structure of the Catalytic and Cytochrome Domains in a Eukaryotic Pyrroloquinoline Quinone-Dependent Dehydrogenase.真核吡咯喹啉醌依赖型脱氢酶的催化和细胞色素结构域的晶体结构。
Appl Environ Microbiol. 2019 Nov 27;85(24). doi: 10.1128/AEM.01692-19. Print 2019 Dec 15.
5
The separate roles of PQQ and apo-enzyme syntheses in the regulation of glucose dehydrogenase activity in Klebsiella pneumoniae NCTC 418.吡咯喹啉醌(PQQ)和脱辅基酶合成在肺炎克雷伯菌NCTC 418葡萄糖脱氢酶活性调节中的独立作用。
Arch Microbiol. 1989;151(3):257-60. doi: 10.1007/BF00413139.
6
Replacement of methoxatin by 4,7-phenanthroline-5,6-dione and the inability of other phenanthroline quinones, as well as 7,9-di-decarboxy methoxatin, to serve as cofactors for the methoxatin-requiring glucose dehydrogenase of Acinetobacter calcoaceticus.用4,7-菲咯啉-5,6-二酮替代甲氧喋呤,以及其他菲咯啉醌类化合物和7,9-二脱羧甲氧喋呤不能作为醋酸钙不动杆菌中需要甲氧喋呤的葡萄糖脱氢酶的辅因子。
Biochem Biophys Res Commun. 1985 Sep 16;131(2):564-6. doi: 10.1016/0006-291x(85)91273-2.
7
Energy transduction by electron transfer via a pyrrolo-quinoline quinone-dependent glucose dehydrogenase in Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter calcoaceticus (var. lwoffi).大肠杆菌、铜绿假单胞菌和乙酸钙不动杆菌(鲁氏变种)中通过依赖于吡咯并喹啉醌的葡萄糖脱氢酶进行电子转移的能量转换
J Bacteriol. 1985 Aug;163(2):493-9. doi: 10.1128/jb.163.2.493-499.1985.
8
Reconstitution of glucose dehydrogenases using synthetic methoxatin.使用合成的甲氧蝶呤对葡萄糖脱氢酶进行重组。
Arch Biochem Biophys. 1982 Oct 15;218(2):623-5. doi: 10.1016/0003-9861(82)90389-7.
9
Reversible thermal inactivation of the quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus. Ca2+ ions are necessary for re-activation.乙酸钙不动杆菌中醌蛋白葡萄糖脱氢酶的可逆热失活。钙离子对再激活是必需的。
Biochem J. 1989 Jul 15;261(2):415-21. doi: 10.1042/bj2610415.
10
Reconstitution of membrane-integrated quinoprotein glucose dehydrogenase apoenzyme with PQQ and the holoenzyme's mechanism of action.膜整合醌蛋白葡萄糖脱氢酶脱辅酶与吡咯喹啉醌的重组及全酶的作用机制。
Biochemistry. 1998 May 12;37(19):6810-8. doi: 10.1021/bi9722610.

引用本文的文献

1
Characterization of the membrane quinoprotein glucose dehydrogenase from Escherichia coli and characterization of a site-directed mutant in which histidine-262 has been changed to tyrosine.大肠杆菌膜结合醌蛋白葡萄糖脱氢酶的特性以及组氨酸-262突变为酪氨酸的定点突变体的特性。
Biochem J. 1999 Jun 15;340 ( Pt 3)(Pt 3):639-47.
2
Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens.基于嗜甲基菌甲醇脱氢酶结构构建的大肠杆菌醌蛋白葡萄糖脱氢酶结构。
Biochem J. 1995 Dec 15;312 ( Pt 3)(Pt 3):679-85. doi: 10.1042/bj3120679.
3
Methanol dehydrogenase: mechanism of action.
甲醇脱氢酶:作用机制
Antonie Van Leeuwenhoek. 1989 May;56(1):25-34. doi: 10.1007/BF00822581.