A structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases.
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1.9 Å structure of the signal receiver domain of the putative response regulator NarL fromMycobacterium tuberculosisStructural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathwayCloning, purification and crystallization of Bacillus anthracis class C acid phosphatase.Pharmacogenetic characterization of naturally occurring germline NT5C1A variants to chemotherapeutic nucleoside analogsIdentification of a New Phosphatase Enzyme Potentially Involved in the Sugar Phosphate Stress Response in Pseudomonas fluorescens.In Vitro and in Silico Evidence of Phosphatase Diversity in the Biomineralizing Bacterium Ramlibacter tataouinensis.Identification and characterization of a plastidial phosphatidylglycerophosphate phosphatase in Arabidopsis thaliana.
P2860
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P2860
A structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases.
description
2005 nî lūn-bûn
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name
A structure-based proposal for ...... erfamily of phosphohydrolases.
@en
A structure-based proposal for ...... erfamily of phosphohydrolases.
@nl
type
label
A structure-based proposal for ...... erfamily of phosphohydrolases.
@en
A structure-based proposal for ...... erfamily of phosphohydrolases.
@nl
prefLabel
A structure-based proposal for ...... erfamily of phosphohydrolases.
@en
A structure-based proposal for ...... erfamily of phosphohydrolases.
@nl
P2093
P1476
A structure-based proposal for ...... perfamily of phosphohydrolases
@en
P2093
Costantino Forleo
Manuela Benvenuti
Stefano Mangani
Vito Calderone
P304
P356
10.1016/J.JMB.2005.10.068
P407
P577
2005-11-10T00:00:00Z