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Dipyrromethane cofactor assembly of porphobilinogen deaminase: formation of apoenzyme and preparation of holoenzyme.

作者信息

Shoolingin-Jordan P M, Warren M J, Awan S J

机构信息

Department of Biochemistry, School of Biological Science, University of Southampton, United Kingdom.

出版信息

Methods Enzymol. 1997;281:317-27. doi: 10.1016/s0076-6879(97)81038-5.

DOI:10.1016/s0076-6879(97)81038-5
PMID:9250996
Abstract
摘要

相似文献

1
Dipyrromethane cofactor assembly of porphobilinogen deaminase: formation of apoenzyme and preparation of holoenzyme.
Methods Enzymol. 1997;281:317-27. doi: 10.1016/s0076-6879(97)81038-5.
2
Discovery that the assembly of the dipyrromethane cofactor of porphobilinogen deaminase holoenzyme proceeds initially by the reaction of preuroporphyrinogen with the apoenzyme.发现胆色素原脱氨酶全酶的二吡咯甲烷辅因子的组装最初是通过尿卟啉原与脱辅基酶的反应进行的。
Biochem J. 1996 Jun 1;316 ( Pt 2)(Pt 2):373-6. doi: 10.1042/bj3160373.
3
Discovery of a novel mechanism for cofactor assembly by Escherichia coli porphobilinogen deaminase.
Biochem Soc Trans. 1997 Feb;25(1):79S. doi: 10.1042/bst025079s.
4
Dipyrromethane cofactor assembly in porphobilinogen deaminase.
Biochem Soc Trans. 1998 Aug;26(3):S286. doi: 10.1042/bst026s286.
5
Reconstitution of apo-porphobilinogen deaminase: structural changes induced by cofactor binding.脱辅基胆色素原脱氨酶的重组：辅因子结合诱导的结构变化。
FEBS Lett. 1989 Jan 2;242(2):319-24. doi: 10.1016/0014-5793(89)80493-4.
6
Reconstitution of the holoenzyme form of Escherichia coli porphobilinogen deaminase from apoenzyme with porphobilinogen and preuroporphyrinogen: a study using circular dichroism spectroscopy.利用圆二色光谱法研究大肠杆菌胆色素原脱氨酶全酶形式从脱辅基酶与胆色素原及尿卟啉原前体的重构。
Biochemistry. 1997 Jul 29;36(30):9273-82. doi: 10.1021/bi9702602.
7
The three-dimensional structure of Escherichia coli porphobilinogen deaminase at 1.76-A resolution.大肠杆菌胆色素原脱氨酶1.76埃分辨率下的三维结构
Proteins. 1996 May;25(1):48-78. doi: 10.1002/(SICI)1097-0134(199605)25:1<48::AID-PROT5>3.0.CO;2-G.
8
Investigation into the nature of substrate binding to the dipyrromethane cofactor of Escherichia coli porphobilinogen deaminase.大肠杆菌胆色素原脱氨酶二吡咯甲烷辅因子与底物结合性质的研究。
Biochemistry. 1988 Dec 13;27(25):9020-30. doi: 10.1021/bi00425a021.
9
Purification, crystallization and properties of porphobilinogen deaminase from a recombinant strain of Escherichia coli K12.来自大肠杆菌K12重组菌株的胆色素原脱氨酶的纯化、结晶及性质
Biochem J. 1988 Sep 1;254(2):427-35. doi: 10.1042/bj2540427.
10
Human porphobilinogen deaminase mutations in the investigation of the mechanism of dipyrromethane cofactor assembly and tetrapyrrole formation.在二吡咯甲烷辅因子组装和四吡咯形成机制研究中对人胆色素原脱氨酶突变的研究
Biochem Soc Trans. 2003 Jun;31(Pt 3):731-5. doi: 10.1042/bst0310731.

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Structural studies of domain movement in active-site mutants of porphobilinogen deaminase from Bacillus megaterium.巨大芽孢杆菌胆色素原脱氨酶活性位点突变体中结构域运动的结构研究
Acta Crystallogr F Struct Biol Commun. 2017 Nov 1;73(Pt 11):612-620. doi: 10.1107/S2053230X17015436. Epub 2017 Oct 30.
2
Structural evidence for the partially oxidized dipyrromethene and dipyrromethanone forms of the cofactor of porphobilinogen deaminase: structures of the Bacillus megaterium enzyme at near-atomic resolution.胆色素原脱氨酶辅因子部分氧化的二吡咯亚甲基和二吡咯甲酮形式的结构证据：巨大芽孢杆菌酶近原子分辨率结构
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3
Conformational stability and activity analysis of two hydroxymethylbilane synthase mutants, K132N and V215E, with different phenotypic association with acute intermittent porphyria.
两种羟甲基胆色素原合酶突变体 K132N 和 V215E 的构象稳定性和活性分析，与急性间歇性卟啉症的不同表型关联。
Biosci Rep. 2013 Aug 8;33(4):e00056. doi: 10.1042/BSR20130045.