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Pyruvate kinase from yeast

Aust, A. Yun, S.L. Suelter, C.H. Pyruvate kinase from yeast (Saccharo-myces cerevisiae). Methods EnzymoL, 42C, 176-182 (1975)... [Pg.62]

Treatment of 9-(/ -D-ribofuranosyluronic acid)adenine with diphenylphosphoro-chloridate and orthophosphate or tripolyphosphate yields (62) and (63), which, although unstable, inhibit rabbit AMP aminohydrolase and pyruvate kinase, respectively, with behaviour characteristic of active-site-specific reagents.98 Adenylate kinases from several sources are inactivated by iV6-[2- and 4-fluorobenzoyl]-adenosine-5 -triphosphates, with kinetics characteristic of active-site labelling, although these compounds were without effect on yeast hexokinase and rabbit pyruvate kinase.99... [Pg.166]

Affinity Labeling of Catalytic ATP Sites. Residues involved in ATP binding are potentially revealed by the use of affinity labels that are based on ATP s structure. Perhaps the most systematically studied of these compounds is 5 -fluorosulfonylbenzoyladenosine (5 -FSBA) (Figure 3a), which has been reported to label at least six kinases (32-A1). In the case of rabbit muscle pyruvate kinase such work has Indicated the presence of a tyrosine residue within the metal nucleotide binding site and an essential cysteine residue located at or near the free metal binding site (32). A similar reagent, 5 -FSBGuanosine, revealed the presence of two cysteine residues at the catalytic site of this same enzyme, both distinct residues from those modified by 5 -FSBA (33,34). With yeast pyruvate kinase both tyrosine and cysteine residues were modified by 5 -FSBA at the catalytic site ( ), and with porcine cAMP-dependent protein kinase a lysine residue was labeled at the active site (36). [Pg.194]

Strick, C.A. James, L.C. O Donnell, M.M. Gollaher, M.G. Franke, A.E. The isolation and characterization of the pyruvate kinase-encoding gene from the yeast Yarrowia lipolytica [published erratum appears in Gene 1994 Mar 11 140(1) 141]. Gene, 118, 65-72 (1992)... [Pg.63]

Mn -ATP (from a folded chelate to an extended outer-sphere complex) when the nucleotide binds to pyruvate kinase. It has also been established that the substitution-inert complex Cr iL-ATP binds at the ATP binding site of the pyruvate kinase-M + complex, and studies with this magnetic probe have led to the construction of molecular models for composite complexes of this important enzyme. Steady-state kinetic studies on the Mn +-, Ni +-, and Co +-activated systems suggest that the substrates of pyruvate kinase are PEP, uncomplexed ADP, and free bivalent cations. Magnesium-complexed ADP and ATP bind at the same site on yeast phosphoglycerate kinase, as do the uncomplexed nucleotides. [Pg.282]

From Sigma 3-aminoethylcarbazole (AEC) acrylamide/bis-acrylamide (30%) 37.5 1 amino acids alumina bentonite benzamidine bovine fiver tRNA bovine serum albumin (BSA) creatine phosphate (CP) diethyl pyrocarbonate (DEPC) dithiothreitol (DTT) Escherichia coli MRE600 tRNA pyrophosphatase (Ppase) Ca++ salt of folinic acid, (5-formyl THF) IIHPHS K salt of phospho-enol pyruvic acid, (PEP) creatine phospho kinase (CPK) protease inhibitor cocktail for fungal and yeast extracts phenylmethylsulfonyl fluoride (PMSF) spermidine trihydrochloride Tween 20. [Pg.262]


See other pages where Pyruvate kinase from yeast is mentioned: [Pg.171]    [Pg.413]    [Pg.196]    [Pg.111]    [Pg.237]    [Pg.124]    [Pg.168]    [Pg.614]    [Pg.169]    [Pg.36]    [Pg.112]    [Pg.129]    [Pg.329]    [Pg.392]    [Pg.63]    [Pg.233]    [Pg.336]    [Pg.57]    [Pg.535]    [Pg.184]    [Pg.76]   


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