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

AuthorLuo, 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
SourceBIOCHEMISTRY-MOSCOW
Issued Date2010-05-01
Volume75Issue:5Pages:655-664
KeywordAnabaena sp PCC7120 phosphorous starvation alkaline phosphatase metalloenzyme site-directed mutagenesis
ISSN0006-2979
Corresponding AuthorZhou, YF, Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China
AbstractAlkaline 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.
English AbstractAlkaline 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.
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
SubjectBiochemistry & Molecular Biology
WOS SubjectBiochemistry & Molecular Biology
WOS Subject ExtendedBiochemistry & Molecular Biology
WOS Keyword PlusSTRAIN PCC 7942 ; ESCHERICHIA-COLI ; ACTIVE-SITE ; PHOSPHORUS LIMITATION ; CRYSTAL-STRUCTURE ; CATALYTIC-ACTIVITY ; REACTION-MECHANISM ; ATLANTIC-OCEAN ; ZINC-BINDING ; SYSTEM
SponsorshipNational Basic Research Program of China [2008CB418000]; Chinese Academy of Sciences ; State Key Laboratory Funds
Indexed TypeSCI
Language英语
WOS IDWOS:000279568800017
Available Date2010-12-23