Abstract 2565 Characterizing the substrate selectivity of guanidine carboxylase and urea carboxylase

Understanding the molecular principles governing enzyme substrate selectivity lays the foundation for engineering enzymes capable of catalyzing reactions on novel substrates with applications in areas such as environmental remediation and drug discovery. Such efforts benefit from a fundamental understanding of how enzymes select their substrates. The urea carboxylase enzyme family offers a compelling case study in substrate selectivity between the homologous enzymes, urea carboxylase (UC) and guanidine carboxylase (GC).

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109209
Primary Topic
Biotin and Related Studies
Type
article
Field-Weighted Citation Impact
0.00
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article

Abstract 2565 Characterizing the substrate selectivity of guanidine carboxylase and urea carboxylase

Martin St. Maurice, Nneamaka Uba
Journal of Biological Chemistry
Biotin and Related Studies
article

Abstract 2565 Characterizing the substrate selectivity of guanidine carboxylase and urea carboxylase

Martin St. Maurice, Nneamaka Uba
article en

Abstract

Understanding the molecular principles governing enzyme substrate selectivity lays the foundation for engineering enzymes capable of catalyzing reactions on novel substrates with applications in areas such as environmental remediation and drug discovery. Such efforts benefit from a fundamental understanding of how enzymes select their substrates. The urea carboxylase enzyme family offers a compelling case study in substrate selectivity between the homologous enzymes, urea carboxylase (UC) and guanidine carboxylase (GC).

Journal of Biological ChemistryVol. 301(5)
Marquette University (US)
Openalex Percentile: Top 86%
Biotin and Related Studies
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