1966
DOI: 10.1016/0076-6879(66)09132-8
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[116] 6-phosphogluconic dehydrase

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Cited by 17 publications
(7 citation statements)
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“…The enzyme is inhibited by fluoride ions. Meloche and Wood [7] provided evidence that the mechanism of action, of EDD involves an enoI-KDPG intermediate that undergoes spontaneous rearrangement to the keto form by a reaction sequence that is essentially irreversible. Purification of the EDD from Zymomonas mobilis indicated that the enzyme functions as a dimer of identical 63-kDa subunits [8].…”
Section: 36-phosphogluconate Dehydratasementioning
confidence: 99%
“…The enzyme is inhibited by fluoride ions. Meloche and Wood [7] provided evidence that the mechanism of action, of EDD involves an enoI-KDPG intermediate that undergoes spontaneous rearrangement to the keto form by a reaction sequence that is essentially irreversible. Purification of the EDD from Zymomonas mobilis indicated that the enzyme functions as a dimer of identical 63-kDa subunits [8].…”
Section: 36-phosphogluconate Dehydratasementioning
confidence: 99%
“…6-Phosphogluconate dehydratase and 2-keto-3-deoxy-6phosphogluconate (KDPG) aldolase, the two enzymes comprising the pathway (see Figure 1), have been characterized extensively in P. putida by W. A. Wood and his coworkers (64,65,83,84). Kersters & De Ley have examined the distribution of these enzymes in a variety of gram-negative bacteria (61,62).…”
Section: Central Role Of the Entner-doudoroff Pathwaymentioning
confidence: 99%
“…Enzyme activities were measured at room temperature in a Gilford 2400 recording spectrophotometer. Published procedures for glucose dehydrogenase (6), glucose-6-phosphate dehydrogenase (8), glucokinase (1), and gluconate-6-phosphate dehydrase (12) were used with minor modifications to provide optimal conditions of pH and substrate concentration. Gluconate dehydrogenase has been assayed by the same method as glucose dehydrogenase but with gluconate as substrate.…”
mentioning
confidence: 99%
“…2-Keto-3-deoxy-gluconate-6-phosphate (KDGP) aldolase activity was measured as described by Meloche et al (11). The substrate for the reaction, KDGP, was produced from gluconate-6-phosphate by means of a KDGP aldolase-free preparation of gluconate-6-phosphate dehydrase, purified from extracts of strain 412-6 (Table 1) by following the procedure of Meloche and Wood (12). The reaction mixture to produce KDGP contained in a final volume of 10 ml: 500 umol of Tris-hydrochloride buffer, pH 8.0; 100 ;&mol of reduced glutathione; 5 Mumol of MnCls; 100 gmol of gluconate-6-phosphate; and 4 international units (IU) of the dehydrase.…”
mentioning
confidence: 99%