PHOSPHORYLATION OF D-GLUCOSE IN ESCHERICHIA-COLI MUTANTS DEFECTIVE IN GLUCOSEPHOSPHOTRANSFERASE, MANNOSEPHOSPHOTRANSFERASE, AND GLUCOKINASE
PHOSPHORYLATION OF D-GLUCOSE IN ESCHERICHIA-COLI MUTANTS DEFECTIVE IN GLUCOSEPHOSPHOTRANSFERASE, MANNOSEPHOSPHOTRANSFERASE, AND GLUCOKINASE
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DOI：
10.1128/jb.122.3.1189-1199.1975
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发表时间：
1975-01-01
影响因子：
3.2
通讯作者：
EPSTEIN, W
中科院分区：
文献类型：
--
作者：
CURTIS, SJ;EPSTEIN, W
遗传学研究表明，大肠杆菌有三种能够磷酸化葡萄糖的酶：可溶性三磷酸腺苷依赖性葡萄糖激酶，在葡萄糖代谢中仅起次要作用;一种酶II，称为葡萄糖磷酸转移酶，对D-葡萄糖构型具有高度特异性;另一种酶II，称为甘露糖磷酸转移酶，具有更广泛的特异性。前一种酶II对葡萄糖和甲基-α-吡喃葡萄糖苷有活性，而后者对D-葡萄糖、D-甘露糖、2-脱氧-D-葡萄糖、D-葡糖胺和D-甘露糖胺有活性。导致葡萄糖磷酸转移酶活性丧失的突变（用符号gpt表示）位于以前称为cat的基因座中的purB和pyrC标记之间。导致甘露糖磷酸转移酶mpt丧失的突变基因座位于eda和fadD基因之间。葡萄糖激酶glk缺失突变位于ptsl和dsd基因之间。
Genetic studies show that Escherichia coli has three enzymes capable of phosphorylating glucose: soluble adenosine 5'-triphosphate-dependent glucokinase, which plays only a minor role in glucose metabolism; an enzyme II, called glucosephosphotransferase, with high specificity for the D-glucose configuration; and another enzyme II, called mannosephosphotransferase, with broader specificity. The former enzyme II is active on glucose and methyl-alpha-glucopyranoside, whereas the latter is active on D-glucose, D-mannose, 2-deoxy-D-glucose, D-glucosamine, and D-mannosamine. Mutations leading to loss of glucosephosphotransferase activity and designated by the symbol gpt are between the purB and pyrC markers in a locus previously called cat. The locus of mutations to loss of mannosephosphotransferase, mpt, is between the eda and fadD genes. Mutations to loss of glucokinase, glk, are between the ptsI and dsd genes.