Escherichia coli pyruvate dehydrogenase complex

CaJacob. C. A., Frey. P. A., Hainfeld, J. F., Wall, J. S., and Yang, H. (1985). Escherichia coli pyruvate dehydrogenase complex. Particle masses of the complex and component enzymes measured by scanning transmission electron microscopy. Biochemistry 24, 2425-2431. [Pg.161]

Apfel MA, Ikeda BH, Speckhard DC et al (1984) Escherichia coli pyruvate dehydrogenase complex. Thiamin pyrophosphate-dependent inactivation by 3-bromopyruvate. J Biol Chem 259 2905-2909... [Pg.42]

Maldonado ME, Oh KJ, Frey PA (1972) Studies on Escherichia coli pyruvate dehydrogenase complex I. Effect of bromopyruvate on the catalytic activities of the complex. J Biol Chem 247 2711-2716... [Pg.42]

Nemeria N, Yan Y, Zhang Z et al (2001) Inhibition of the Escherichia coli pyruvate dehydrogenase complex El subunit and its tyrosine 177 variants by thiamin 2-thiazolone and thiamin 2-thiothiazolone diphosphates. Evidence for reversible tight-binding inhibition. J Biol Chem 276 45969 5978... [Pg.42]

He JB, Feng LL, Li J et al (2012) Design, s5mthesis and biological evaluation of novel 2-methylpyrimidine-4-ylamine derivatives as inhibitors of Escherichia coli pyruvate dehydrogenase complex El. Bioorg Med Chem 20 1665-1670... [Pg.42]

Schonbrunn-Hanebeck E, Laber B, Amrhein N (1990) Slow-binding inhibition of the Escherichia coli pyruvate dehydrogenase multienzyme complex by acetylphosphinate. Biochemistry 29 4880-4885... [Pg.42]

Nemeria NS, Korotchkina LG, Chakraborty S et al (2(X)6) Acetylphosphinate is the most potent mechanism-based substrate-like inhibitor of both the human and Escherichia coli pyruvate dehydrogenase components of the pymvate dehydrogenase complex. Bioorg Chem 34 362-379... [Pg.43]

The pyruvate dehydrogenase complex from Escherichia coli is considerably more complex than tryptophan synthetase. It has a molecular weight of approximately 4.6 millon and contains three enzymes pyruvate dehydrogenase (Et), dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3).82 The overall reaction catalyzed by the complex is... [Pg.201]

Y.-H. Park, Protein Interactions in the Pyruvate Dehydrogenase Complex from Escherichia coli. Ph.D. Thesis, Rutgers University Graduate Faculty at Newark, NJ, 2008. [Pg.597]

Thiamine pyrophosphate (18) Affinity chromatography of the pyruvate dehydrogenase complex of wild type Escherichia coli 254... [Pg.533]

Kim, Y, Ingram, L.O., and Shanmugam, K.T. (2008) Dihydrolipoamide dehydrogenase mutation alters the NADH sensitivity of pyruvate dehydrogenase complex of Escherichia coli K-12. J. Bacteriol, 190, 3851—3858. [Pg.570]

Murarka A, Clomburg JM, Moran S et al (2010) Metabolic analysis of wild-type Escherichia coli and a pyruvate dehydrogenase complex (PDHC)-deficient derivative reveals the role of PDHC in the fermentative metabolism of glucose. J Biol Chem 285 31548-31558... [Pg.40]

Stephens PE, Darlison MG, Lewis HW et al (1983) The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the pyruvate dehydrogenase component Eur J Biochem 133 155-162... [Pg.40]

Lowe PN, Perham RN (1984) Bromopyruvate as an active-site-directed inhibitor of the pyruvate dehydrogenase multienzyme complex from Escherichia coli. Biochemistry 23 91-97 Bisswanger H (1980) Fluoropyruvate a potent inhibitor of the bacterial and the mammalian pyruvate dehydrogenase complex. Biochem Biophys Res Commun 95 513-519... [Pg.42]

Flournoy DS, Frey PA (1989) Inactivation of the pyruvate dehydrogenase complex of Escherichia coli by fluoropyruvate. Biochemistry 28 9594-9602... [Pg.42]

Akiyama, S. K, and Hamme.s, G. G., 1981. Elementary. steps in die reaction mechani.sm of die pyruvate dehydrogenase mnltienzyme complex from Escherichia coli Kinetics of flavin reduction. Biochemistry 20 1491-1497. [Pg.672]

The PDH complex contains three enzymes—pyruvate dehydrogenase (EJ, dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3)—each present in multiple copies. The number of copies of each enzyme and therefore the size of the complex varies among species. The PDH complex isolated from mammals is about 50 nm in diameter—more than five times the size of an entire ribosome and big enough to be visualized with the electron microscope (Fig. 16-5a). In the bovine enzyme, 60 identical copies of E2 form a pentagonal dodecahedron (the core) with a diameter of about 25 nm (Fig. 16-5b). (The core of the Escherichia coli enzyme contains 24 copies of E2.) E2 is the point of... [Pg.604]

It should be noted that some anaerobic eubacteria (e.g. Escherichia coli, Clostridium acidurici, Chlorobium limicold) possess 2-oxoacid oxidoreductases, either in addition to, or instead of, the dehydrogenase complexes (ref. [37] and references therein). As in the archaebacteria, electrons are transferred to ferredoxin or flavodoxin and the enzymes are small oligomeric proteins. The evolutionary relationships of these enzymes converting pyruvate to acetyl-CoA will be discussed in section 6.2. [Pg.8]

Figure 1 Fermentation pathways of Escherichia coli. Gene symbols ackA, acetate kinase adhE, alcohol dehydrogenase fdh, formate dehydrogenase of FHL complex fhn, nitrate-inducible formate dehydrogenase hyd, hydrogenase 3 of FHL complex IdhA, NAD+-dependent D-(-)-lactate dehydrogenase pfl, pyruvate formate-lyase pta, phosphotransacetylase. FHL, formate hydrogenlyase. Redrawn from reference 29...

Jones, D. D., Horne, H. J., Reche, P. A., and Perham, R. N. 2000. Structural determinants of post-translational modification and catalytic specificity for the lipoyi domains of the pyruvate dehydrogenase multienzyme complex of Escherichia coli. J. Mot. Biol. 295 289-306. [Pg.498]

Arjunan, P, Chandrasekhar, K., Sax, M., et al. (2004) Structural determinants of enzyme binding affinity The El component of pyruvate dehydrogenase from Escherichia coli in complex with the inhibitor thiamin thiazolone diphosphate. Biochemistry 43,2405-2411. [Pg.120]

Deprotonation Rate of the C2-H of Thiamin Diphosphate in the Pyruvate Dehydrogenase Multienzyme Complex from Escherichia coli... [Pg.1425]

Akiyama, S. K., Hammes, G. G. (1980), Elementary steps in the reaction mechanism of the pyruvate dehydrogenase multienzyme complex from Escherichia coli kinetics of acetylation and deacetylation, Biochemistry 19, 4208-4213. [Pg.1436]

This compound is the product of oxidation of the enamine by any one of the following oxidizing agents on enzymes most commonly by the dithiolane ring of lipoic acid covalently amidated to a lysine side chain in the 2-oxoacid dehydrogenase multienzyme complexes less frequently by FAD in the pyruvate oxidases — these come in two flavors, forming acetate in Escherichia coli and forming acetylphosphate in L. plantarum, finally by NAD. ... [Pg.577]

Saumweber H, Binder R, BisswangCT H (1981) Pyruvate dehydrogenase component of the p)nuvate dehydrogenase complex from Escherichia coli K12. Purification and characterization. Eur J Biochem 114 407—411... [Pg.40]

Aijunan P, Nemeria N, Branskill A et al (2002) Stracture of the pyruvate dehydrogenase multienzyme complex El component from Escherichia coli at 1.85 A resolution. Biochemistry 41 5213-5221... [Pg.41]

Stevenson KJ, Hale G, Perham RN (1978) Inhibition of pyruvate dehydrogenase multienzyme complex from Escherichia coli with mono- and bifunctional arsenoxides. Biochemistry 17 2189-2192... [Pg.41]

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