The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor
The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor
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DOI：
10.1093/emboj/20.10.2480
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发表时间：
2001-05-15
期刊：
影响因子：
11.4
通讯作者：
Erni, B
中科院分区：
文献类型：
--
作者：
Gutknecht, R;Beutler, R;Erni, B
大肠杆菌的二羟基丙酮激酶（DhaK）由三个可溶性蛋白亚基组成，DhaK （YcgT; 39.5 kDa）和DhaL （YcgS; 22.6 kDa）与细菌、动物和植物中普遍存在的atp依赖性DhaK的N端和c端半相似。同二聚体DhaM （YcgC; 51.6 kDa）由三个结构域组成。细菌磷酸烯醇丙酮酸糖磷酸转移酶系统（PTS）甘露糖转运体的n端二聚化结构域与IIA结构域（PDB代码1PDO）具有相同的折叠，中间结构域与HPr相似，c端与PTS I酶（EI）的n端结构域相似，DhaM在EI和HPr依赖的反应中被磷酸烯醇丙酮酸磷酸化三次。DhaK和DhaL不被磷酸化，DhaM的IIA结构域，而不是ATP，是二羟基丙酮（Dha）的磷酸化供体，与PTS的碳水化合物特异性转运体不同，DhaK、DhaL和DhaM没有转运活性。
The dihydroxyacetone kinase (DhaK) of Escherichia coli consists of three soluble protein subunits, DhaK (YcgT; 39.5 kDa) and DhaL (YcgS; 22.6 kDa) are similar to the N- and C-terminal halves of the ATP-dependent DhaK ubiquitous in bacteria, animals and plants. The homodimeric DhaM (YcgC; 51.6 kDa) consists of three domains. The N-terminal dimerization domain has the same fold as the IIA domain (PDB code 1PDO) of the mannose transporter of the bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS), The middle domain is similar to HPr and the C-terminus is similar to the N-terminal domain of enzyme I (EI) of the PTS, DhaM is phosphorylated three times by phosphoenolpyruvate in an EI- and HPr-dependent reaction. DhaK and DhaL are not phosphorylated, The IIA domain of DhaM, instead of ATP, is the phosphoryl donor to dihydroxyacetone (Dha), Unlike the carbohydrate-specific transporters of the PTS, DhaK, DhaL and DhaM have no transport activity.