18 Enolase

Wold, Finn

doi:10.1016/s1874-6047(08)60101-8

Cited by 106 publications

(79 citation statements)

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“…Enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) is a metalloenzyme that catalyses the dehydration of 2-phospho-D-glycerate (2-PGA) to phosphoenolpyruvate (PEP) in the forward or catabolic direction in the second half of the EmbdenMayerhoff-Parnas glycolytic pathway [1]. During gluconeogenesis (anabolic pathway) the same enzyme as a phosphopyruvate hydratase catalyses the reverse reaction hydration of PEP to 2-PGA.…”

Section: Introductionmentioning

confidence: 99%

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Inhibition of human muscle-specific enolase by methylglyoxal and irreversible formation of advanced glycation end products

Gamian

Staniszewska

Danielewicz

2009

Journal of Enzyme Inhibition and Medicinal Chemistry

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Methylglyoxal (MG) was studied as an inhibitor and effective glycating factor of human muscle-specific enolase. The inhibition was carried out by the use of a preincubation procedure in the absence of substrate. Experiments were performed in anionic and cationic buffers and showed that inhibition of enolase by methylglyoxal and formation of enolasederived glycation products arose more effectively in slight alkaline conditions and in the presence of inorganic phosphate. Incubation of 15 micromolar solutions of the enzyme with 2 mM, 3.1 mM and 4.34 mM MG in 100 mM phosphate buffer pH 7.4 for 3 h caused the loss a 32%, 55% and 82% of initial specific activity, respectively. The effect of MG on catalytic properties of enolase was investigated. The enzyme changed the K M value for glycolytic substrate 2-phospho-D-glycerate (2-PGA) from 0.2 mM for native enzyme to 0.66 mM in the presence of MG. The affinity of enolase for gluconeogenic substrate phosphoenolpyruvate altered after preincubation with MG in the same manner, but less intensively. MG has no effect on V max and optimal pH values. Incubation of enolase with MG for 0-48 h generated high molecular weight protein derivatives. Advanced glycation end products (AGEs) were resistant to proteolytic degradation by trypsin. Magnesium ions enhanced the enzyme inactivation by MG and facilitated AGEs formation. However, the protection for this inhibition in the presence of 2-PGA as glycolytic substrate was observed and AGEs were less effectively formed under these conditions.

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Section: Introductionmentioning

confidence: 99%

“…The native enolase molecule is a hetero-or homodimer formed by two subunits from of a, b, or g type of monomer which are encoded by three different loci in the majority of human and mammals tissues. In skeletal muscles, the bb isoenzyme predominates (over 90% of total enolase activity) [1,3].…”

Section: Introductionmentioning

confidence: 99%

Inhibition of human muscle-specific enolase by methylglyoxal and irreversible formation of advanced glycation end products

Gamian

Staniszewska

Danielewicz

2009

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…Enolase catalyses the conversion of 2-phosphoglycerate into phosphoenolpyruvate, substrate of the second ATP-generating reaction. In addition to the main mutase activity, PGM possesses collateral 2,3-bisphosphoglycerate synthase or 2,3-bisphosphoglycerate mutase activity (BPGM: 1,3-bisphosphoglycerate + 3-phosphoglycerate -> 3-phosphoglycerate + 2,3-bisphosphoglycerate) and 2,3-bisphosphoglycerate phosphatase activity (BPGP: 2,3-bisphosphoglycerate --3-phosphoglycerate + Pi), which is stimulated by 2-phosphoglycolate (for reviews, see Fothergill-Gilmore and Watson, 1989;Wold, 1971).In mammalian tissues, there are three isoenzymes of PGM, which result from the homodimeric and the heterodimeric combinations of two different subunits coded by separate genes and designated M (muscle) and B (brain). In early fetal life, type BB-PGM is the only form present.…”

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confidence: 99%

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas

Durany

Joseph²,

Campo³

et al. 1997

Br J Cancer

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SummaryWe have compared the levels of phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activities and the distribution of their isoenzymes in normal colon, liver and lung tissues, and in colon, liver and lung adenocarcinoma, lung squamous cell carcinoma and lung carcinoid. All tumours presented higher phosphoglycerate mutase and enolase activities and lower 2,3-bisphosphoglycerate phosphatase activity than the normal tissues. No changes were observed in the phosphoglycerate mutase isoenzyme patterns analysed by cellulose acetate electrophoresis. All specimens contained mainly type BB isoenzyme, traces of type MB isoenzyme and no type MM isoenzyme. However, the tumours had decreased levels of 2,3-bisphosphoglycerate mutase and 2,3-bisphosphoglycerate mutase-phosphoglycerate mutase hybrid enzyme. Determined by agarose gel electrophoresis, aa-enolase was the isoenzyme predominant in normal lung, colon and liver tissue, although ay-and yy-enolase were also present in all tissues. In colon, liver and non-endocrine lung tumours, the proportions of ay-and yy-enolase decreased. In contrast, in carcinoid tumours of the lung, the proportions of these isoenzymes increased.Keywords: 2,3-bisphosphoglycerate mutase; 2,3-bisphosphoglycerate phosphatase; enolase; phosphoglycerate mutase; isoenzyme; lung, colon and liver adenocarcinoma; lung squamous cell carcinoma; lung carcinoid Phosphoglycerate mutase (D-phosphoglycerate 2,3-phosphomutase, EC 5.4.2.1, PGM) and enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) are glycolytic enzymes that catalyse consecutive reversible reactions connecting the two ATP-generating reactions in the glycolytic pathway. PGM catalyses the conversion of 3-phosphoglycerate, product of the first ATP-generating reaction, into 2-phosphoglycerate in the presence of the cofactor 2,3-bisphosphoglycerate. Enolase catalyses the conversion of 2-phosphoglycerate into phosphoenolpyruvate, substrate of the second ATP-generating reaction. In addition to the main mutase activity, PGM possesses collateral 2,3-bisphosphoglycerate synthase or 2,3-bisphosphoglycerate mutase activity (BPGM: 1,3-bisphosphoglycerate + 3-phosphoglycerate -> 3-phosphoglycerate + 2,3-bisphosphoglycerate) and 2,3-bisphosphoglycerate phosphatase activity (BPGP: 2,3-bisphosphoglycerate --3-phosphoglycerate + Pi), which is stimulated by 2-phosphoglycolate (for reviews, see Fothergill-Gilmore and Watson, 1989;Wold, 1971).In mammalian tissues, there are three isoenzymes of PGM, which result from the homodimeric and the heterodimeric combinations of two different subunits coded by separate genes and designated M (muscle) and B (brain). In early fetal life, type BB-PGM is the only form present. During myogenesis, the isoenzyme phenotype undergoes transition, type BB-PGM being replaced by the MM-form, through the MB isoenzyme. In skeletal muscle, there is an almost complete transition from the BB-to the MM-PGM, but in heart muscle complete transition does not occur (Omenn and Cheung, Omenn and Hermodson, 1975;Adamson, 1...

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“…This difference may simply be due to differences between the active sites of these two enzymes, as has been observed previously (Wold, 1971).…”

Section: Enzyme Inhibition Studiesmentioning

confidence: 57%

Inhibition of glycolytic enzymes by 2-phosphotartronate

Thomas

Spring

1976

Biochemical Journal

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18 Enolase

Cited by 106 publications

References 54 publications

Inhibition of human muscle-specific enolase by methylglyoxal and irreversible formation of advanced glycation end products

Inhibition of human muscle-specific enolase by methylglyoxal and irreversible formation of advanced glycation end products

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas

Inhibition of glycolytic enzymes by 2-phosphotartronate

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