The gene ygdP, associated with the invasiveness of Escherichia coli K1, designates a Nudix hydrolase, Orf176, active on adenosine (5')-pentaphospho-(5')-adenosine (Ap5A).
The gene ygdP, associated with the invasiveness of Escherichia coli K1, designates a Nudix hydrolase, Orf176, active on adenosine (5')-pentaphospho-(5')-adenosine (Ap5A).
复制标题
基因 ygdP 与大肠杆菌 K1 的侵袭性相关,指定 Nudix 水解酶 Orf176,对腺苷 (5)-五磷酸-(5)-腺苷 (Ap5A) 具有活性。
DOI:
--
复制
发表时间:
2001
影响因子:
4.8
通讯作者:
Jianying Shen
中科院分区:
文献类型:
--
作者:
M. Bessman;J. Walsh;Christopher A. Dunn;Jyothishmathi Swaminathan;John E. Weldon;Jianying Shen
ygdP, a gene associated with the invasion of brain microvascular endothelial cells by Escherichia coli K1 (Badger, J. L., Wass, C. A., and Kim, K. S. (2000) Mol. Microbiol. 36, 174-182), the primary Gram-negative bacterium causing meningitis in newborns, has been cloned and expressed in E. coli. The protein, YgdP, was purified to near homogeneity and identified as a member of the Nudix hydrolase subfamily of dinucleoside oligophosphate pyrophosphatases. It catalyzes the hydrolysis of diadenosine tetra-, penta-, and hexa-phosphates with a preference for diadenosine penta-phosphate, from which it forms ATP and ADP. The enzyme has a requirement for a divalent metal cation that can be met with Mg2+, Zn2+, or Mn2+ and, like most of the Nudix hydrolases, has an alkaline pH optimum between 8.5 and 9. This is the second identification of a gene associated with the invasiveness of a human pathogen as a member of the Nudix hydrolase subfamily of dinucleoside oligophosphate pyrophosphatases, and an examination of homologous proteins in other invasive bacteria suggests that this may be a common feature of cellular invasion.
DOI:
10.1073/pnas.80.24.7496
发表时间:
1983-01-01
期刊:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子:
--
作者:
LEE, PC;BOCHNER, BR;AMES, BN
通讯作者:
AMES, BN
DOI:
10.1006/bbrc.1999.0354
发表时间:
1999-03-24
影响因子:
3.1
作者:
Cartwright, JL;Britton, P;McLennan, AG
通讯作者:
McLennan, AG