Molecular cloning and characterization of a novel adenylate kinase 3 gene from Clonorchis sinensis

被引:27
|
作者
Yang, G
Yu, XB
Wu, ZD
Xu, J
Song, LX
Zhang, HM
Hu, XC
Zheng, NC
Guo, LC
Xu, J
Dai, JF
Ji, CN
Gu, SH
Ying, K
机构
[1] Sun Yat Sen Univ, Sch Med, Dept Parasitol, Guangzhou 510089, Peoples R China
[2] Minist Educ, Key Lab Trop Dis Control, Guangzhou 510089, Peoples R China
[3] Fudan Univ, Sch Life Sci, Inst Genet, State Key Lab Genet Engn, Shanghai 200433, Peoples R China
关键词
D O I
10.1007/s00436-005-1305-y
中图分类号
R38 [医学寄生虫学]; Q [生物科学];
学科分类号
07 ; 0710 ; 09 ; 100103 ;
摘要
Adenylate kinase (AK) is a ubiquitous enzyme that contributes to the homeostasis of adenine nucleotides in living cells. AK catalyzes reversible high energy phosphoryl transfer reactions between ATP ( or GTP) and AMP to generate ADP ( or GDP). From a Clonorchis sinensis adult worm cDNA library, we isolated a cDNA clone encoding a novel AK3 isozyme. The 956 bp cDNA encodes a putative protein of 228 amino acids with a predicted molecular mass of 26.2 kDa. The recombinant CsAK3 protein produced in Escherichia coli can be refolded into a functional protein with AK3 activity. The optimum pH and temperature for the enzyme are 8.5 and 40 degrees C, respectively. The calculated activation energy is 56.04 kJ mol(-1). The K-m of the CsAK3 for AMP and GTP are 118 mu M and 359 mu M, respectively. CsAK3 is inhibited by Ap5A (> 70% inhibition by 2.0 mM AP(5)A). Ap(5)A may be a potential lead compound acting on C. sinensis in which AK3 as a drug target.
引用
收藏
页码:406 / 412
页数:7
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