Molecular Physiology of Phosphoryl Group Transfer from Carbamoyl Phosphate by a Hyperthermophilic Enzyme at Low Temperature
Author:
Affiliation:
1. Instituto de Biomedicina de Valencia (CSIC), Jaume Roig 11, 46010-Valencia, Spain
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi011637d
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1. Relation between stability, dynamics and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus
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2. New Insight into the Transcarbamylase Family: The Structure of Putrescine Transcarbamylase, a Key Catalyst for Fermentative Utilization of Agmatine;PLoS ONE;2012-02-20
3. Substrate Binding and Catalysis in Carbamate Kinase Ascertained by Crystallographic and Site-Directed Mutagenesis Studies: Movements and Significance of a Unique Globular Subdomain of This Key Enzyme for Fermentative ATP Production in Bacteria;Journal of Molecular Biology;2010-04
4. The Gene Cluster for Agmatine Catabolism of Enterococcus faecalis : Study of Recombinant Putrescine Transcarbamylase and Agmatine Deiminase and a Snapshot of Agmatine Deiminase Catalyzing Its Reaction;Journal of Bacteriology;2007-02-15
5. First-time crystallization and preliminary X-ray crystallographic analysis of a bacterial-archaeal type UMP kinase, a key enzyme in microbial pyrimidine biosynthesis;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2005-03
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