CHARACTERIZATION OF 2 GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE ISOENZYMES FROM THE PENTALENOLACTONE PRODUCER STREPTOMYCES-ARENAE
CHARACTERIZATION OF 2 GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE ISOENZYMES FROM THE PENTALENOLACTONE PRODUCER STREPTOMYCES-ARENAE
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DOI：
10.1128/jb.153.2.930-936.1983
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发表时间：
1983-01-01
影响因子：
3.2
通讯作者：
MECKE, D
中科院分区：
文献类型：
--
作者：
MAURER, KH;PFEIFFER, F;MECKE, D
Pentalenolactone (PL) 不可逆地灭活 3-磷酸甘油醛脱氢酶 [D-3-磷酸甘油醛:NAD+ 氧化还原酶（磷酸化）]，并且是原核和真核细胞中糖酵解的有效抑制剂。 PL 生产菌株 S. arenae TU469 在 PL 生产条件下含有 PL 不敏感的 3-磷酸甘油醛脱氢酶。在复杂培养基中，没有观察到 PL 产生，并且可以检测到 PL 敏感的 3-磷酸甘油醛脱氢酶，而不是不敏感的酶。这些酶具有相同的底物特异性，但催化和分子特性不同。 PL不敏感酶和敏感酶对3-磷酸甘油醛的表观Km值分别为100和250μM，并且在PL不敏感酶不被抑制的条件下，PL敏感酶被PL强烈抑制。 PL 不敏感酶的物理特性表明该蛋白质是八聚体；与其他 3-磷酸甘油醛脱氢酶一样，PL 敏感酶似乎是四聚体。
Pentalenolactone (PL) irreversibly inactivates the enzyme glyceraldehyde-3-phosphate dehydrogenase [D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating)] and is a potent inhibitor of glycolysis in both prokaryotic and eukaryotic cells. PL-producing strain, S. arenae TU469, contains a PL-insensitive glyceraldehyde-3-phosphate dehydrogenase under conditions of PL production. In complex media, no PL production was observed and a PL-sensitive glyceraldehyde-3-phosphate dehydrogenase, rather than the insensitive enzyme, could be detected. The enzymes had the same substrate specificity, but different catalytic and molecular properties. The apparent Km values of the PL-insensitive and sensitive enzymes for glyceraldehyde-3-phosphate were 100 and 250 .mu.M, respectively, and the PL-sensitive enzyme was strongly inhibited by PL under conditions in which the PL-insensitive enzyme was not inhibited. The physical properties of the PL-insensitive enzyme suggest that the protein is an octamer; the PL-sensitive enzyme, like other glyceraldehyde-3-phosphate dehydrogenases, appears to be a tetramer.