ArticleProtein science : a publication of the Protein Society2005
Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 82 citations in OpenAlex.
- Enhancing stability of enzymes for industrial applications: molecular insights and emerging approaches.World journal of microbiology & biotechnology · 2025Review
- Classification of Acid and Alkaline Enzymes Based on Normalized Van der Waals Volume Features.Proteomics. Clinical applications · 2025Article
- Enzymatic Treatment of Lignin in Alkaline Homogeneous Systems: A Review on Alkaliphilic Laccases.ChemSusChem · 2025Review
- A Deep Retrieval-Enhanced Meta-Learning Framework for Enzyme Optimum pH Prediction.Journal of chemical information and modeling · 2025Article
- Metagenomic mining unveils a novel GH130 enzyme with exclusive xylanase activity over a wide temperature and pH ranges.Journal of industrial microbiology & biotechnology · 2024Article
- Extremozyme-Based Biosensors for Environmental Pollution Monitoring: Recent Developments.Biosensors · 2024Review
- Living in trinity of extremes: Genomic and proteomic signatures of halophilic, thermophilic, and pH adaptation.Current research in structural biology · 2024Article
- L-serine biosynthesis in the human central nervous system: Structure and function of phosphoserine aminotransferase.Protein science : a publication of the Protein Society · 2023Article
- Molecular Structure of Phosphoserine Aminotransferase fromInternational journal of molecular sciences · 2023Article
- Adaptation of neutrophilic Paracoccus denitrificans to denitrification at highly alkaline pH.Environmental science and pollution research international · 2020Article
- Influence of Hydrogen Electron Donor, Alkaline pH, and High Nitrate Concentrations on Microbial Denitrification: A Review.International journal of molecular sciences · 2019Review
- Crystal Structure of a Highly Thermostable α-Carbonic Anhydrase from Persephonella marina EX-H1.Molecules and cells · 2019Article
- Structural adaptations of octaheme nitrite reductases from haloalkaliphilic Thioalkalivibrio bacteria to alkaline pH and high salinity.PloS one · 2017Article
- A new alkaline lipase obtained from the metagenome of marine sponge Ircinia sp.World journal of microbiology & biotechnology · 2015Article
- Structural Insight into and Mutational Analysis of Family 11 Xylanases: Implications for Mechanisms of Higher pH Catalytic Adaptation.PloS one · 2015Article
- Draft Genome Sequence of Bacillus alcalophilus AV1934, a Classic Alkaliphile Isolated from Human Feces in 1934.Genome announcements · 2014Article
- AcalPred: a sequence-based tool for discriminating between acidic and alkaline enzymes.PloS one · 2013Article
- Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that support the ability to grow in an external pH range from 7.5 to 11.4.Environmental microbiology · 2011Article
- Structural analysis of alkaline β-mannanase from alkaliphilic Bacillus sp. N16-5: implications for adaptation to alkaline conditions.PloS one · 2011Article
- Entamoeba histolytica Phosphoserine aminotransferase (EhPSAT): insights into the structure-function relationship.BMC research notes · 2010Article
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3 authors at 1 institution in 1 country.
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Abstract
The crystal structure of the vitamin B(6)-dependent enzyme phosphoserine aminotransferase from the obligatory alkaliphile Bacillus alcalophilus has been determined at 1.08 A resolution. The model was refined to an R-factor of 11.7% (R(free) = 13.9%). The enzyme displays a narrow pH optimum of enzymatic activity at pH 9.0. The final structure was compared to the previously reported structure of the mesophilic phosphoserine aminotransferase from Escherichia coli and to that of phosphoserine aminotransferase from a facultative alkaliphile, Bacillus circulans subsp. alkalophilus. All three enzymes are homodimers with each monomer comprising a two-domain architecture. Despite the high structural similarity, the alkaliphilic representatives possess a set of distinctive structural features. Two residues directly interacting with pyridoxal-5'-phosphate are replaced, and an additional hydrogen bond to the O3' atom of the cofactor is present in alkaliphilic phosphoserine aminotransferases. The number of hydrogen bonds and hydrophobic interactions at the dimer interface is increased. Hydrophobic interactions between the two domains in the monomers are enhanced. Moreover, the number of negatively charged amino acid residues increases on the solvent-accessible molecular surface and fewer hydrophobic residues are exposed to the solvent. Further, the total amount of ion pairs and ion networks is significantly reduced in the Bacillus enzymes, while the total number of hydrogen bonds is increased. The mesophilic enzyme from Escherichia coli contains two additional beta-strands in a surface loop with a third beta-strand being shorter in the structure. The identified structural features are proposed to be possible factors implicated in the alkaline adaptation of phosphoserine aminotransferase.
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