X-ray crystallographic and site-directed mutagenesis analysis of the mechanism of Schiff-base formation in phosphonoacetaldehyde hydrolase catalysis (Q27642769)

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English	X-ray crystallographic and site-directed mutagenesis analysis of the mechanism of Schiff-base formation in phosphonoacetaldehyde hydrolase catalysis	scientific article

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scholarly article

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X-ray crystallographic and site-directed mutagenesis analysis of the mechanism of Schiff-base formation in phosphonoacetaldehyde hydrolase catalysis (English)

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Debra Dunaway-Mariano

5

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author name string

Marc C Morais

1

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Guofeng Zhang

2

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Wenhai Zhang

3

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David B Olsen

4

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Karen N Allen

6

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language of work or name

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publication date

5 March 2004

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Journal of Biological Chemistry

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279

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10

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9353-61

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Phosphonates and their degradation by microorganisms

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In vitro characterization of a phosphate starvation-independent carbon-phosphorus bond cleavage activity in Pseudomonas fluorescens 23F.

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The enzymic cleavage of the carbon-phosphorus bond: Purification and properties of phosphonatase

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Investigation of the Bacillus cereus phosphonoacetaldehyde hydrolase. Evidence for a Schiff base mechanism and sequence analysis of an active-site peptide containing the catalytic lysine residue

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Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis

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The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Processing of X-ray diffraction data collected in oscillation mode

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Determination of protein molecular weight, hydration, and packing from crystal density

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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

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Improved methods for building protein models in electron density maps and the location of errors in these models

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PROCHECK: a program to check the stereochemical quality of protein structures

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Detection, delineation, measurement and display of cavities in macromolecular structures

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Kinetic evidence for a substrate-induced fit in phosphonoacetaldehyde hydrolase catalysis

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The CCP4 suite: programs for protein crystallography

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PK of the lysine amino group at the active site of acetoacetate decarboxylase

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Mechanism of the reaction catalyzed by acetoacetate decarboxylase. Importance of lysine 116 in determining the pKa of active-site lysine 115

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A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases

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Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 A(,)

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Snapshots of catalysis: the structure of fructose-1,6-(bis)phosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate

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Observation of covalent intermediates in an enzyme mechanism at atomic resolution

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Covalent intermediate trapped in 2-keto-3-deoxy-6- phosphogluconate (KDPG) aldolase structure at 1.95-A resolution

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In vitro cleavage of the carbon-phosphorus bond of phosphonopyruvate by cell extracts of an environmental Burkholderia cepacia isolate

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Acetoacetate decarboxylase. Identification of the rate-determining step in the primary amine catalyzed reaction and in the enzymic reaction

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Crystallization and preliminary crystallographic analysis of phosphonoacetaldehyde hydrolase

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The molecular replacement method

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Implementation of molecular replacement in AMoRe

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Reporter group at the active site of acetoacetate decarboxylase. II. Ionization constant of the amino group

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Investigation of the substrate binding and catalytic groups of the P-C bond cleaving enzyme, phosphonoacetaldehyde hydrolase

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10.1074/JBC.M312345200

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