Structures of enzyme-bound metal-nucleotide complexes in the phosphoryl transfer reaction of muscle pyruvate kinase. 31P NMR studies with magnesium and kinetic studies with chromium nucleotides.

Gupta, Raj K.; Mildvan, A S

doi:10.1016/s0021-9258(17)40014-7

Cited by 68 publications

(31 citation statements)

References 27 publications

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“…The picture of the pyruvate kinase active site which is presently available is one where there are two nearby divalent metals (Gupta et al, 1976; Gupta & Mildvan, 1977;Baek & Nowak, 1982; Muirhead et al, 1986;Lodato & Reed, 1987; Buchbinder & Reed, 1990). We refer to the binding sites for the two nearby divalent metals as site I and site II.…”

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confidence: 99%

Electron nuclear double resonance study of the manganese(2+) environs in the oxalate-ATP complex of pyruvate kinase

Tan

Poyner²,

Reed³

et al. 1993

Biochemistry

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Electron nuclear double resonance (ENDOR) and the related pulse technique of pulse field sweep EPR (PFSEPR) were used to probe the site I environment of Mn2+ in the oxalate-ATP complex of pyruvate kinase. Assignment of features and an estimate of hyperfine couplings have shown proximity of protons to the metal ions through their dipolar interaction and proximity of 31P and 17O because of a contact interaction from direct Mn(2+)-ligand covalent spin transfer. Since Mn2+ is a spin5/2 ion whose Ms = +/- 1/2, +/- 3/2, and +/- 5/2 electron spin states can all contribute to EPR and ENDOR, we have developed experimental and theoretical strategies for elucidating hyperfine couplings to the Mn2+ electron spin states. Solvent-exchangeable proton ENDOR features were evident with couplings very similar to the hyperfine couplings of H2O in [Mn(H2O)6]2+. ENDOR of exchangeable, more distant protons originated from a dipolar coupling such as could be expected from protons residing 5.5 A from Mn2+ and hydrogen-bonded to a nonliganding oxygen or nitrogen. Nonexchangeable proton ENDOR features indicated dipolar coupling to proton(s) from the protein residing at approximately 4.5 A from the Mn2+. The approximately 4-MHz 31P phosphate hyperfine couplings in Mn(II)-nucleotide models and in pyruvate kinase were similar, but a detailed ENDOR and PFSEPR comparison revealed that the hyperfine coupling to the ATP gamma-phosphate in pyruvate kinase was approximately 10% less than coupling to phosphates of Mn(II)-nucleotides. [In pyruvate kinase only the gamma-phosphate has been shown to bind to Mn2+ at site I (Lodato & Reed, 1987).](ABSTRACT TRUNCATED AT 250 WORDS)

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confidence: 99%

Electron nuclear double resonance study of the manganese(2+) environs in the oxalate-ATP complex of pyruvate kinase

Tan

Poyner²,

Reed³

et al. 1993

Biochemistry

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“…Complexes of ATP with pyruvate kinase are attractive candidates for detailed studies of the binding interactions involving the terminal phosphoryl group of the nucleoside triphosphate. The enzyme needs 2 equiv of divalent metal ion (Gupta et al, 1976; Gupta & Mildvan, 1977;Baek & Nowak, 1982) and a monovalent cation (Boyer et al, 1942) per active site for activity, and all three of these inorganic ions are positioned within the active site. In complexes with ATP and oxalate, an analogue of enolpyruvate, the 7-phosphoryl group of ATP is a bridging ligand for the two divalent cations (Lodato & Reed, 1987; Buchbinder & Reed, 1990).…”

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confidence: 99%

Stereochemistry of metal ion coordination to the terminal thiophosphoryl group of adenosine 5'-O-(3-thiotriphosphate) at the active site of pyruvate kinase

Buchbinder

Baraniak²,

Frey³

et al. 1993

Biochemistry

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Epimers of [gamma-17O]adenosine 5'-O-(3-thiotriphosphate) ([gamma-17O]ATP gamma S) have been used to determine the stereochemistry of Mn2+ coordination to the terminal thiophosphoryl group in complexes of pyruvate kinase, oxalate, ATP gamma S, and Mg2+, Zn2+, Co2+, or Cd2+. The complex of pyruvate kinase with oxalate and ATP binds 2 equiv of divalent cation per active site. The terminal phosphoryl group of ATP in this enzymic complex becomes a chiral center as a result of coordination to both divalent metal ions. Electron paramagnetic resonance (EPR) data for complexes of pyruvate kinase with Rp- or Sp-[gamma-17O]-ATP gamma S, [17O]oxalate, and mixtures of Mn2+ with Mg2+, Zn2+, or Co2+ show that Mn2+ binds selectively at the site defined by coordination to oxalate and the pro-R oxygen of the thiophosphoryl group of ATP gamma S. In mixtures containing Mn2+ and Cd2+ with Tl+ as the monovalent cation, two hybrid complexes form, enzyme-oxalate-MnII-ATP gamma S-CdII and enzyme-oxalate-CdII-ATP gamma S-MnII, as in the analogous complexes with ATP and K+ or Tl+ (Buchbinder, J. L., & Reed, G. H. (1990) Biochemistry 29, 1799-1806). In the enzyme-oxalate-MnII-ATP gamma S-CdII species, Mn2+ binds exclusively to the pro-R oxygen of the thiophosphoryl group. In the enzyme-oxalate-CdII-ATP gamma S-MnII species, Mn2+ binds to the pro-R oxygen (60%) and to the pro-S oxygen (40%).(ABSTRACT TRUNCATED AT 250 WORDS)

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“…variety of kinetic and magnetic resonance techniques, have revealed the requirement for two divalent cations per active site (Gupta et al, 1976a,b;Gupta & Mildvan, 1977). One of these divalent cations binds to the enzyme and forms second-sphere complexes with the bound substrates while the second binds directly to the triphosphate chain of the ATP (Gupta et al, 1976a,b;Gupta & Mildvan, 1977).…”

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confidence: 99%

Stereospecificity of the metal-adenosine 5'-triphosphate complex in reactions of muscle pyruvate kinase

Dunaway‐Mariano¹,

Benovic²,

Cleland³

et al. 1979

Biochemistry

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Structures of enzyme-bound metal-nucleotide complexes in the phosphoryl transfer reaction of muscle pyruvate kinase. 31P NMR studies with magnesium and kinetic studies with chromium nucleotides.

Cited by 68 publications

References 27 publications

Electron nuclear double resonance study of the manganese(2+) environs in the oxalate-ATP complex of pyruvate kinase

Electron nuclear double resonance study of the manganese(2+) environs in the oxalate-ATP complex of pyruvate kinase

Stereochemistry of metal ion coordination to the terminal thiophosphoryl group of adenosine 5'-O-(3-thiotriphosphate) at the active site of pyruvate kinase

Stereospecificity of the metal-adenosine 5'-triphosphate complex in reactions of muscle pyruvate kinase

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