ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
X-ray structure and characterization of carbamate kinase from the human parasite Giardia lamblia.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Article
- Metabolic cooperation supports mutual growth between the protozoan parasite Trichomonas vaginalis and dysbiotic vaginal bacteria.PLoS pathogens · 2026Article
- TheJournal of microbiology and biotechnology · 2022Article
- Enzymology of the pathway for ATP production by arginine breakdown.The FEBS journal · 2021Article
- Discovery and Preclinical Development of Antigiardiasis Fumagillol Derivatives.Antimicrobial agents and chemotherapy · 2020Article
- Structural basis for inactivation of Giardia lamblia carbamate kinase by disulfiram.The Journal of biological chemistry · 2014Article
- Crystal structures of carbamate kinase from Giardia lamblia bound with citric acid and AMP-PNP.PloS one · 2013Article
- Structural characterization of the enzymes composing the arginine deiminase pathway in Mycoplasma penetrans.PloS one · 2012Article
- A homogenous luminescence assay reveals novel inhibitors for giardia lamblia carbamate kinase.Current chemical genomics · 2012Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Carbamate kinase catalyzes the reversible conversion of carbamoyl phosphate and ADP to ATP and ammonium carbamate, which is hydrolyzed to ammonia and carbonate. The three-dimensional structure of carbamate kinase from the human parasite Giardia lamblia (glCK) has been determined at 3 A resolution. The crystals belonged to the monoclinic space group P2(1), with unit-cell parameters a = 69.77, b = 85.41, c = 102.1 A, beta = 106.8 degrees . The structure was refined to a final R factor of 0.227. The essentiality of glCK together with its absence in humans makes the enzyme an attractive candidate for anti-Giardia drug development. Steady-state kinetic rate constants have been determined. The k(cat) for ATP formation is 319 +/- 9 s(-1). The K(m) values for carbamoyl phosphate and ADP are 85 +/- 6 and 70 +/- 5 microM, respectively. The structure suggests that three invariant lysine residues (Lys131, Lys216 and Lys278) may be involved in the binding of substrates and phosphoryl transfer. The structure of glCK reveals that a glycerol molecule binds in the likely carbamoyl phosphate-binding site.
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