ArticleThe protein journal2010
Identification and characterization of a putative dihydroorotase, KPN01074, from Klebsiella pneumoniae.
Article in The protein journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Conformational Dynamics of the Active Site Loop in Dihydroorotase Highlighting the Limitations of Loop-In Structures for Inhibitor Docking.International journal of molecular sciences · 2025Article
- Bioactive Potential ofPlants (Basel, Switzerland) · 2025Article
- Plumbagin, a Natural Product with Potent Anticancer Activities, Binds to and Inhibits Dihydroorotase, a Key Enzyme in Pyrimidine Biosynthesis.International journal of molecular sciences · 2021Article
- Structural Basis for pH-Dependent Oligomerization of Dihydropyrimidinase fromBioinorganic chemistry and applications · 2018Article
- Characterization of the Dihydroorotase from Methanococcus jannaschii.The protein journal · 2017Article
- Ca-asp bound X-ray structure and inhibition of Bacillus anthracis dihydroorotase (DHOase).Bioorganic & medicinal chemistry · 2016Article
- Article
- The mononuclear metal center of type-I dihydroorotase from Aquifex aeolicus.BMC biochemistry · 2013Article
- High-level expression, purification, and characterization of Staphylococcus aureus dihydroorotase (PyrC) as a cleavable His-SUMO fusion.Protein expression and purification · 2013Article
- Characterization of flavonol inhibition of DnaB helicase: real-time monitoring, structural modeling, and proposed mechanism.Journal of biomedicine & biotechnology · 2012Article
- Biochemical characterization of allantoinase from Escherichia coli BL21.The protein journal · 2011Article
- Characterization of a single-stranded DNA binding protein from Salmonella enterica serovar Typhimurium LT2.The protein journal · 2011Article
- Characterization of a single-stranded DNA-binding protein from Pseudomonas aeruginosa PAO1.The protein journal · 2011Article
- Inhibition of Klebsiella pneumoniae DnaB helicase by the flavonol galangin.The protein journal · 2011Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dihydroorotase (DHO; EC 3.5.2.3) is an essential metalloenzyme in the biosynthesis of pyrimidine nucleotides. Here, we identified and characterized DHO from the pathogenic bacterium Klebsiella pneumoniae (Kp). The activity of KpDHO toward L: -dihydroorotate was observed with K (m) = 0.04 mM and V (max) = 8.87 mumol/(mg min). Supplementing the standard growth medium with Co2+, Mn2+, Mg2+, or Ni2+ increased enzyme activity. The catalytic activity of KpDHO was inhibited with Co2+, Zn2+, Mn2+, Cd2+, Ni2+, and phosphate ions. Substituting the putative metal binding residues His17, His19, Lys103, His140, His178, and Asp251 with Ala completely abolished KpDHO activity. However, the activity of the mutant D251E was fourfold higher than that of the wild-type protein. On the basis of these biochemical and mutational analyses, KpDHO (KPN01074) was identified as type II DHO.
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