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Cited by 18Biochemical and Molecular ResearchAmino Acid Enzymes and MetabolismChemical Reaction Mechanisms

Characterization of a Novel dUTP-Dependent Activity of CTP Synthetase from Saccharomyces cerevisiae

Pappas, Apostolos, Park, Tae-Sik, Carman, George M.·1999·Biochemistry
DOI 10.1021/bi9920127
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Abstract

CTP synthetase [EC 6.3.4.2, UTP:ammonia ligase (ADP-forming)] from the yeast Saccharomyces cerevisiae catalyzes the ATP-dependent transfer of the amide nitrogen from glutamine to the C-4 position of UTP to form CTP. In this work, we demonstrated that CTP synthetase utilized dUTP as a substrate to synthesize dCTP. The dUTP-dependent activity was linear with time and with enzyme concentration. Maximum dUTP-dependent activity was dependent on MgCl(2) (4 mM) and GTP (K(a) = 14 microM) at a pH optimum of 8.0. The apparent K(m) values for dUTP, ATP, and glutamine were 0.18, 0.25, and 0.41 mM, respectively. dUTP promoted the tetramerization of CTP synthetase, and the extent of enzyme tetramerization correlated with dUTP-dependent activity. dCTP was a poor inhibitor of dUTP-dependent activity, whereas CTP was a potent inhibitor of this activity. The enzyme catalyzed the synthesis of dCTP and CTP when dUTP and UTP were used as substrates together. CTP was the major product synthesized when dUTP and UTP were present at saturating concentrations. When dUTP and UTP were present at concentrations near their K(m) values, the synthesis of dCTP increased relative to that of CTP. The synthesis of dCTP was favored over the synthesis of CTP when UTP was present at a concentration near its K(m) value and dUTP was varied from subsaturating to saturating concentrations. These data suggested that the dUTP-dependent synthesis of dCTP by CTP synthetase activity may be physiologically relevant.

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  • In S. cerevisiae and Lactococcus lactis, their respective CTP synthases have activity toward dUTP.

    “In other organisms such as S. cerevisiae and Lactococcus lactis, their respective CTP synthases have activity toward dUTP Pappas et al. (1999); Willemoës and Sigurskjold (2002).”

    From Fundamental behaviors emerge from simulations of a living minimal cell (2022) · cites this paper as Pappas et al. (1999)

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Authors
Pappas, A., Park, T.-S., & Carman, G. M.
Affiliations
Rutgers, The State University of New Jersey (US)
Corresponding author
Carman, George M.
ORCID
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1999-11-24
Volume
38
Issue
50
Pages
16671-16677
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi9920127
OpenAlex
W2125945123
Cited by
18
References
28
Citations by year
2024: 3 · 2022: 1 · 2020: 1 · 2019: 1 · 2013: 1
FWCI
0.46
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
  • Rutgers University Community Repository (Rutgers University) (submittedVersion)
Funders
  • National Institutes of Health
  • U.S. Public Health Service
  • National Institute of General Medical Sciences (GM-50679, R01GM050679)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
  • Physical Sciences › Chemistry › Organic Chemistry › Chemical Reaction Mechanisms
Keywords
CTP synthase, UTP, glutamine, enzyme inhibition, substrate specificity, Saccharomyces cerevisiae, nucleotide metabolism
MeSH terms
Chromatography, High Pressure Liquid, Cytidine Triphosphate, Deoxycytosine Nucleotides, Deoxyuracil Nucleotides, Enzyme Activation, Kinetics, Saccharomyces cerevisiae, Substrate Specificity, Dimerization, Carbon-Nitrogen Ligases

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