ArticleBiochemistry2010
Discovery and structure determination of the orphan enzyme isoxanthopterin deaminase .
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 18 citations in OpenAlex.
- Structural and mechanistic insights into the divergence of pterin deaminase and sepiapterin deaminase.Applied microbiology and biotechnology · 2026Review
- Biosynthesis of Pteridines in Insects: A Review.Insects · 2024Review
- Structural Determinants for Substrate Selectivity in Guanine Deaminase Enzymes of the Amidohydrolase Superfamily.Biochemistry · 2019Article
- Substrate Profile of the Phosphotriesterase Homology Protein from Escherichia coli.Biochemistry · 2018Article
- Detection of 224 candidate structured RNAs by comparative analysis of specific subsets of intergenic regions.Nucleic acids research · 2017Article
- Coping with inevitable accidents in metabolism.Microbial biotechnology · 2017Review
- Article
- Article
- Deamination of 6-aminodeoxyfutalosine in menaquinone biosynthesis by distantly related enzymes.Biochemistry · 2013Article
- The orphan protein bis-γ-glutamylcystine reductase joins the pyridine nucleotide disulfide reductase family.Biochemistry · 2013Article
- Assignment of pterin deaminase activity to an enzyme of unknown function guided by homology modeling and docking.Journal of the American Chemical Society · 2013Article
- Structure-based function discovery of an enzyme for the hydrolysis of phosphorylated sugar lactones.Biochemistry · 2012Article
- Discovery of a cytokinin deaminase.ACS chemical biology · 2011Article
- Pa0148 from Pseudomonas aeruginosa catalyzes the deamination of adenine.Biochemistry · 2011Article
- Rescue of the orphan enzyme isoguanine deaminase.Biochemistry · 2011Article
- Three-dimensional structure and catalytic mechanism of cytosine deaminase.Biochemistry · 2011Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Two previously uncharacterized proteins have been identified that efficiently catalyze the deamination of isoxanthopterin and pterin 6-carboxylate. The genes encoding these two enzymes, NYSGXRC-9339a ( gi|44585104 ) and NYSGXRC-9236b ( gi|44611670 ), were first identified from DNA isolated from the Sargasso Sea as part of the Global Ocean Sampling Project. The genes were synthesized, and the proteins were subsequently expressed and purified. The X-ray structure of Sgx9339a was determined at 2.7 A resolution (Protein Data Bank entry 2PAJ ). This protein folds as a distorted (beta/alpha)(8) barrel and contains a single zinc ion in the active site. These enzymes are members of the amidohydrolase superfamily and belong to cog0402 within the clusters of orthologous groups (COG). Enzymes in cog0402 have previously been shown to catalyze the deamination of guanine, cytosine, S-adenosylhomocysteine, and 8-oxoguanine. A small compound library of pteridines, purines, and pyrimidines was used to probe catalytic activity. The only substrates identified in this search were isoxanthopterin and pterin 6-carboxylate. The kinetic constants for the deamination of isoxanthopterin with Sgx9339a were determined to be 1.0 s(-1), 8.0 muM, and 1.3 x 10(5) M(-1) s(-1) (k(cat), K(m), and k(cat)/K(m), respectively). The active site of Sgx9339a most closely resembles the active site for 8-oxoguanine deaminase (Protein Data Bank entry 2UZ9 ). A model for substrate recognition of isoxanthopterin by Sgx9339a was proposed on the basis of the binding of guanine and xanthine in the active site of guanine deaminase. Residues critical for substrate binding appear to be conserved glutamine and tyrosine residues that form hydrogen bonds with the carbonyl oxygen at C4, a conserved threonine residue that forms hydrogen bonds with N5, and another conserved threonine residue that forms hydrogen bonds with the carbonyl group at C7. These conserved active site residues were used to identify 24 other genes which are predicted to deaminate isoxanthopterin.
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