中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Characterization of a Monomeric Heat-Labile Classical Alkaline Phosphatase from Anabaena sp PCC7120

文献类型:期刊论文

作者Luo, Ming1,2; Guo, Yong-Chao1; Deng, Jiao-Yu1; Wei, Hong-Ping1; Zhang, Zhi-Ping1; Leng, Yan1,2; Men, Dong1,2; Song, Li-Rong3; Zhang, Xian-En1; Zhou, Ya-Feng1
刊名BIOCHEMISTRY-MOSCOW
出版日期2010-05-01
卷号75期号:5页码:655-664
ISSN号0006-2979
关键词Anabaena sp PCC7120 phosphorous starvation alkaline phosphatase metalloenzyme site-directed mutagenesis
通讯作者Zhou, YF, Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China
中文摘要Alkaline phosphatases (APs), known inducible enzymes of the Pho regulon and poorly characterized in cyanobacteria, hydrolyze phosphomonoesters to produce inorganic phosphate (P-i) during P-i starvation. In this study, two predicted alkaline phosphatase genes in the genome of Anabaena sp. PCC 7120, all2843 and alr5291, were apparently induced during P-i starvation. Sequence analysis showed that alr5291 encodes a protein that is an atypical alkaline phosphatase like other cyanobacteria PhoAs, but the protein encoded by all2843 is very similar to the classical PhoAs, such as Escherichia coli alkaline phosphatase (EAP). To date, there have been no reports about classical phoA in cyanobacterial genomes. The alkaline phosphatase AP(A), coded by all2843, is characterized as a metalloenzyme containing Mg2+ and Zn2+ with molar ratio of 1 : 2. Site-directed mutagenesis analysis indicated that, though the active center of AP(A) is highly conserved in comparison with EAP, differences do exist between AP(A) and EAP in metal ion coordination. Besides, biochemical analysis revealed that AP(A) is a monomeric protein and inactivated rapidly at 50 degrees C. These results suggest that AP(A) is the first monomeric heat-labile classical PhoA found in cyanobacteria.
英文摘要Alkaline phosphatases (APs), known inducible enzymes of the Pho regulon and poorly characterized in cyanobacteria, hydrolyze phosphomonoesters to produce inorganic phosphate (P(i)) during P(i) starvation. In this study, two predicted alkaline phosphatase genes in the genome of Anabaena sp. PCC 7120, all2843 and alr5291, were apparently induced during P(i) starvation. Sequence analysis showed that alr5291 encodes a protein that is an atypical alkaline phosphatase like other cyanobacteria PhoAs, but the protein encoded by all2843 is very similar to the classical PhoAs, such as Escherichia coli alkaline phosphatase (EAP). To date, there have been no reports about classical phoA in cyanobacterial genomes. The alkaline phosphatase AP(A), coded by all2843, is characterized as a metalloenzyme containing Mg(2+) and Zn(2+) with molar ratio of 1 : 2. Site-directed mutagenesis analysis indicated that, though the active center of AP(A) is highly conserved in comparison with EAP, differences do exist between AP(A) and EAP in metal ion coordination. Besides, biochemical analysis revealed that AP(A) is a monomeric protein and inactivated rapidly at 50 degrees C. These results suggest that AP(A) is the first monomeric heat-labile classical PhoA found in cyanobacteria.
学科主题Biochemistry & Molecular Biology
WOS标题词Science & Technology ; Life Sciences & Biomedicine
类目[WOS]Biochemistry & Molecular Biology
研究领域[WOS]Biochemistry & Molecular Biology
关键词[WOS]STRAIN PCC 7942 ; ESCHERICHIA-COLI ; ACTIVE-SITE ; PHOSPHORUS LIMITATION ; CRYSTAL-STRUCTURE ; CATALYTIC-ACTIVITY ; REACTION-MECHANISM ; ATLANTIC-OCEAN ; ZINC-BINDING ; SYSTEM
资助信息National Basic Research Program of China [2008CB418000]; Chinese Academy of Sciences ; State Key Laboratory Funds
收录类别SCI
语种英语
WOS记录号WOS:000279568800017
公开日期2010-12-23
源URL[http://ir.ihb.ac.cn/handle/342005/13785]  
专题水生生物研究所_藻类生物学及应用研究中心_期刊论文
作者单位1.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China
2.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China
3.Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Peoples R China
推荐引用方式
GB/T 7714
Luo, Ming,Guo, Yong-Chao,Deng, Jiao-Yu,et al. Characterization of a Monomeric Heat-Labile Classical Alkaline Phosphatase from Anabaena sp PCC7120[J]. BIOCHEMISTRY-MOSCOW,2010,75(5):655-664.
APA Luo, Ming.,Guo, Yong-Chao.,Deng, Jiao-Yu.,Wei, Hong-Ping.,Zhang, Zhi-Ping.,...&Zhou, Ya-Feng.(2010).Characterization of a Monomeric Heat-Labile Classical Alkaline Phosphatase from Anabaena sp PCC7120.BIOCHEMISTRY-MOSCOW,75(5),655-664.
MLA Luo, Ming,et al."Characterization of a Monomeric Heat-Labile Classical Alkaline Phosphatase from Anabaena sp PCC7120".BIOCHEMISTRY-MOSCOW 75.5(2010):655-664.

入库方式: OAI收割

来源:水生生物研究所

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