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The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.嗜热甲烷菌坎氏甲烷嗜热菌AV19的全基因组及古生菌产甲烷菌的单系性
Proc Natl Acad Sci U S A. 2002 Apr 2;99(7):4644-9. doi: 10.1073/pnas.032671499.
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Expression in Escherichia coli of the thermostable inorganic pyrophosphatase from the Aquifex aeolicus and purification and characterization of the recombinant enzyme.嗜热栖热菌耐热无机焦磷酸酶在大肠杆菌中的表达及重组酶的纯化与特性分析
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Quaternary structure and metal ion requirement of family II pyrophosphatases from Bacillus subtilis, Streptococcus gordonii, and Streptococcus mutans.枯草芽孢杆菌、戈登链球菌和变形链球菌中II族焦磷酸酶的四级结构和金属离子需求
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Genomic sequence of hyperthermophile, Pyrococcus furiosus: implications for physiology and enzymology.嗜热菌激烈火球菌的基因组序列：对生理学和酶学的启示
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6
Methanococcus jannaschii ORF mj0608 codes for a class C inorganic pyrophosphatase protected by Co(2+) or Mn(2+) ions against fluoride inhibition.詹氏甲烷球菌开放阅读框mj0608编码一种C类无机焦磷酸酶，该酶受Co(2+)或Mn(2+)离子保护，免受氟化物抑制。
Arch Biochem Biophys. 2000 Jul 15;379(2):292-8. doi: 10.1006/abbi.2000.1860.
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Cytoplasmic inorganic pyrophosphatase.细胞质无机焦磷酸酶
Prog Mol Subcell Biol. 1999;23:127-50. doi: 10.1007/978-3-642-58444-2_7.
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The extreme thermostable pyrophosphatase from Sulfolobus acidocaldarius: enzymatic and comparative biophysical characterization.嗜酸热硫化叶菌的极端耐热焦磷酸酶：酶学及比较生物物理特性研究
Arch Biochem Biophys. 1999 Mar 1;363(1):135-47. doi: 10.1006/abbi.1998.1072.
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Cloning and expression of a unique inorganic pyrophosphatase from Bacillus subtilis: evidence for a new family of enzymes.
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10
Bacillus subtilis ORF yybQ encodes a manganese-dependent inorganic pyrophosphatase with distinctive properties: the first of a new class of soluble pyrophosphatase?枯草芽孢杆菌开放阅读框yybQ编码一种具有独特性质的锰依赖性无机焦磷酸酶：一类新型可溶性焦磷酸酶中的首个成员？
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来自嗜热栖热菌OT3的I型无机焦磷酸酶的特性分析。

Characterization of the Family I inorganic pyrophosphatase from Pyrococcus horikoshii OT3.

作者信息

Jeon Sung-Jong, Ishikawa Kazuhiko

机构信息

Department of Biotechnology and Bioengineering, Dong-Eui University, Busan, 614-714, Korea.

出版信息

Archaea. 2005 Dec;1(6):385-9. doi: 10.1155/2005/591628.

DOI:10.1155/2005/591628
PMID:16243777
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2685581/
Abstract

A gene encoding for a putative Family I inorganic pyrophosphatase (PPase, EC 3.6.1.1) from the hyperthermophilic archaeon Pyrococcus horikoshii OT3 was cloned and the biochemical characteristics of the resulting recombinant protein were examined. The gene (Accession No. 1907) from P. horikoshii showed some identity with other Family I inorganic pyrophosphatases from archaea. The recombinant PPase from P. horikoshii (PhPPase) has a molecular mass of 24.5 kDa, determined by SDS-PAGE. This enzyme specifically catalyzed the hydrolysis of pyrophosphate and was sensitive to NaF. The optimum temperature and pH for PPase activity were 70 degrees C and 7.5, respectively. The half-life of heat inactivation was about 50 min at 105 degrees C. The heat stability of PhPPase was enhanced in the presence of Mg2+. A divalent cation was absolutely required for enzyme activity, Mg2+ being most effective; Zn2+, Co2+ and Mn2+ efficiently supported hydrolytic activity in a narrow range of concentrations (0.05-0.5 mM). The K(m) for pyrophosphate and Mg2+ were 113 and 303 microM, respectively; and maximum velocity, V(max), was estimated at 930 U mg(-1).

摘要

克隆了来自嗜热古菌火球菌OT3的一个假定的I类无机焦磷酸酶（PPase，EC 3.6.1.1）的编码基因，并检测了所得重组蛋白的生化特性。火球菌的该基因（登录号1907）与来自古菌的其他I类无机焦磷酸酶有一定的同源性。通过SDS-PAGE测定，来自火球菌的重组PPase（PhPPase）分子量为24.5 kDa。该酶特异性催化焦磷酸水解，对NaF敏感。PPase活性的最适温度和pH分别为70℃和7.5。在105℃下热失活的半衰期约为50分钟。在Mg2+存在下，PhPPase的热稳定性增强。酶活性绝对需要二价阳离子，Mg2+最为有效；Zn2+、Co2+和Mn2+在狭窄的浓度范围（0.05 - 0.5 mM）内有效支持水解活性。焦磷酸和Mg2+的K(m)分别为113和303 μM；最大反应速度V(max)估计为930 U mg(-1)。