Structure of a His170Tyr mutant of thermostable pNPPase from<i>Geobacillus stearothermophilus</i>

Shen, Tiantian; Guo, Zheng; Ji, Chaoneng

doi:10.1107/s2053230x14007341

Cited by 3 publications

(1 citation statement)

References 33 publications

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“…1b), indicating that AfPase is a member of HAD-like superfamily. Moreover, the deduced amino-acid sequence of this phosphatase has modest identities with three identified p-nitrophenyl phosphatase from Saccharomyces cerevisiae (24.2%, NCBI accession CAB56540.1) (Kaneko et al 1989), Bacillus stearothermophilus (30.6%, NCBI accession AAM29189.1) (Shen et al 2014), and Thermoplasma acidophilum (13.6%, NCBI accession WP_110641440.1) (Ekaterina et al 2010). Despite the identities of the whole protein sequence of AfPase with other HAD phosphatases are relatively low, the typical α/β core domains including motif I-IV and a mobile cap domain are highly conserved (Additional file 1: Figure S1).…”

Section: Sequence Analysis Of Afpasementioning

confidence: 99%

Characterization of a hyperthermophilic phosphatase from Archaeoglobus fulgidus and its application in in vitro synthetic enzymatic biosystem

Wang

Meng

et al. 2019

Bioresour. Bioprocess.

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Background: Haloacid dehalogenase (HAD)-like hydrolases represent the largest superfamily of phosphatases, which release inorganic phosphate from phosphate containing compounds, such as sugar phosphates. The HAD-like phosphatases with highly substrate specificity, which perform irreversible dephosphorylation, are always integrated into in vitro synthetic enzymatic biosystems as the last enzymatic step for the cost-efficient production of biochemicals. Therefore, identification and characterization of substrate specificity of HAD-like phosphatases are important for exploring their application. Results: In this study, a hyperthermophilic HAD-like phosphatase from Archaeoglobus fulgidus (AfPase) was cloned, expressed, and characterized. AfPase was identified as a type I Mg 2+-dependent HAD-like phosphatase with high optimal temperature and thermostability. Among the tested phosphate containing compounds, AfPase exhibited the highest catalytic activity on p-nitrophenyl phosphate, followed by dihydroxyacetone phosphate (DHAP). On the basis of the high catalytic activity of AfPase to generate 1,3-dihydroxyacetone (DHA) from DHAP, an in vitro synthetic enzymatic biosystem containing this phosphatase and other five enzymes was constructed for the biosynthesis of DHA from inexpensive maltodextrin in one pot. About 14 mM (1.26 g/L) DHA was produced from 10 g/L maltodextrin. Conclusions: A hyperthermophilic HAD-like phosphatase from Archaeoglobus fulgidus was characterized carefully, and the success of an in vitro synthetic enzymatic biosystem containing this phosphatase provided a promising approach for DHA production from maltodextrin.

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Section: Sequence Analysis Of Afpasementioning

confidence: 99%

Characterization of a hyperthermophilic phosphatase from Archaeoglobus fulgidus and its application in in vitro synthetic enzymatic biosystem

Wang

Meng

et al. 2019

Bioresour. Bioprocess.

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Enzymatic characterization of a thermostable phosphatase from Thermomicrobium roseum and its application for biosynthesis of fructose from maltodextrin

Meng

Liang

Wei

et al. 2019

Appl Microbiol Biotechnol

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High-quality Thermodynamic Data on the Stability Changes of Proteins Upon Single-site Mutations

Pucci

Bourgeas

Rooman

2016

Journal of Physical and Chemical Reference Data

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We have set up and manually curated a dataset containing experimental information on the impact of amino acid substitutions in a protein on its thermal stability. It consists of a repository of experimentally measured melting temperatures (T m) and their changes upon point mutations (∆T m) for proteins having a well-resolved X-ray structure. This high-quality dataset is designed for being used for the training or benchmarking of in silico thermal stability prediction methods. It also reports other experimentally measured thermodynamic quantities when available, i.e. the folding enthalpy (∆H) and heat capacity (∆C P) of the wild type proteins and their changes upon mutations (∆∆H and ∆∆C P), as well as the change in folding free energy (∆∆G) at a reference temperature. These data are analyzed in view of improving our insights into the correlation between thermal and thermodynamic stabilities, the asymmetry between the number of stabilizing and destabilizing mutations, and the difference in stabilization potential of thermostable versus mesostable proteins.

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Structure of a His170Tyr mutant of thermostable pNPPase fromGeobacillus stearothermophilus

Cited by 3 publications

References 33 publications

Characterization of a hyperthermophilic phosphatase from Archaeoglobus fulgidus and its application in in vitro synthetic enzymatic biosystem

Characterization of a hyperthermophilic phosphatase from Archaeoglobus fulgidus and its application in in vitro synthetic enzymatic biosystem

Enzymatic characterization of a thermostable phosphatase from Thermomicrobium roseum and its application for biosynthesis of fructose from maltodextrin

High-quality Thermodynamic Data on the Stability Changes of Proteins Upon Single-site Mutations

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