Alkaline phosphatase is an almost perfect enzyme.

No abstract is available for this paper.

• Publication year

  1994

• Venue

  Biochemistry

• Publication date

  1994-08-30

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1021/BI00200A018PMID 8068674
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  2006cited by this paper
• Catalysis of the hydrolysis of phosphorylated pyridines by alkaline phosphatase has little or no dependence on the pKa of the leaving group.

  1993cited by this paper
• Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues.

  1989cited by this paper
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  1988cited by this paper
• Possible role for water dissociation in the slow binding of phosphorus-containing transition-state-analogue inhibitors of thermolysin.

  1987cited by this paper
• Leaving group dependence in the phosphorylation of Escherichia coli alkaline phosphatase by monophosphate esters.

  1986cited by this paper
• Refined structure of alkaline phosphatase from Escherichia coli at 2.8 A resolution.

  1985cited by this paper
• Alkaline phosphatase. 31P NMR probes of the mechanism.

  1985cited by this paper
• Reactions of pyridines and primary amines with N-phosphorylated pyridines

  1984cited by this paper
• Evidence for a single transition state in the transfer of the phosphoryl group (-PO32-) to nitrogen nucleophiles from pyridinio-N-phosphonates

  1984cited by this paper
• 31P nuclear magnetic resonance of phosphoenzyme intermediates of alkaline phosphatase.

  1983cited by this paper
• Interactions of proteins with solvent components in 8 M urea.

  1981cited by this paper
• Thermodynamic and kinetic examination of protein stabilization by glycerol.

  1981cited by this paper
• The stabilization of proteins by sucrose.

  1981cited by this paper
• Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures.

  1981cited by this paper
• Amino acid sequence of Escherichia coli alkaline phosphatase.

  1981cited by this paper
• Allosteric interactions between metal ion and phosphate at the active sites of alkaline phosphatase as determined by 31P NMR and 113Cd NMR.

  1977cited by this paper
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  1976cited by this paper
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  1976cited by this paper
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  1974cited by this paper
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  1972cited by this paper
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  1972cited by this paper
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  1968cited by this paper
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  1967cited by this paper
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