dGTP triphosphohydrolase, a unique enzyme confined to members of the family Enterobacteriaceae.
dGTP triphosphohydrolase, a unique enzyme confined to members of the family Enterobacteriaceae.
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dGTP 三磷酸水解酶，一种仅限于肠杆菌科成员的独特酶。
DOI：
10.1128/jb.173.21.6665-6669.1991
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发表时间：
1991
影响因子：
3.2
通讯作者：
Bessman,MJ
中科院分区：
文献类型：
--
作者：
Quirk,S;Bessman,MJ
在几个属的细菌的部分纯化的提取物中测定酶dGTP三磷酸水解酶（dGTP酶; EC 3.1.5.1），发现其严格限于肠杆菌科的成员。而12个肠道细菌中有11个对这种酶具有可比活性，8个非肠道细菌中有8个，包括非常密切相关的弧菌属和气单胞菌属中的物种，没有对这种酶进行阳性检测。当挑战与大肠杆菌抗dGT酶抗血清，活性酶分为三组，保留0，约50，或100%的原始活性。计算机搜索揭示了E.大肠杆菌酶，其与Prasad和Chiu的单链DNA结合基序很好地匹配（J. Mol. Biol. 193：579-584，1987），并且可以解释所观察到的酶与DNA的相互作用。据我们所知，这是迄今为止报道的仅存在于肠道细菌中的唯一酶活性。
The enzyme dGTP triphosphohydrolase (dGTPase; EC 3.1.5.1) was assayed in partially purified extracts of several genera of bacteria, and it was found to be strictly confined to members of the family Enterobacteriaceae. Whereas 11 of 12 enteric bacteria had comparable activity for this enzyme, 8 of 8 nonenteric bacteria, including species in the very closely related genera Vibrio and Aeromonas, did not assay positively for this enzyme. When challenged with Escherichia coli anti-dGTPase antiserum, the active enzymes fell into three groups, retaining 0, approximately 50, or 100% of their original activity. A computer search has revealed an amino acid sequence in the E. coli enzyme which matches well with the single-stranded-DNA binding motif of Prasad and Chiu (J. Mol. Biol. 193:579-584, 1987) and may account for the enzyme's observed interaction with DNA. As far as we are aware, this is the only enzymatic activity so far reported to be present solely in the enteric bacteria.