Surveying purine biosynthesis across the domains of life unveils promising drug targets in pathogens

SMH Chua, JA Fraser - Immunology and cell biology, 2020 - Wiley Online Library
Purines play an integral role in cellular processes such as energy metabolism, cell signaling
and encoding the genetic makeup of all living organisms—ensuring that the purine …

The Ureides 6

KR SCHUBERT, MJ BOLAND - Intermediary nitrogen …, 2012 - books.google.com
Ureides are a class of cyclic or acyclic nitrogenous organic compounds derived from or
structurally related to urea. Representatives of this class which have been found in plants …

[HTML][HTML] Gene Networks and Pathways Involved in Escherichia coli Response to Multiple Stressors

EK Abdelwahed, NA Hussein, A Moustafa, NA Moneib… - Microorganisms, 2022 - mdpi.com
Stress response helps microorganisms survive extreme environmental conditions and host
immunity, making them more virulent or drug resistant. Although both reductionist …

Nucleotides, nucleosides, and nucleobases

KF Jensen, G Dandanell, B Hove-Jensen… - EcoSal …, 2008 - Am Soc Microbiol
We review literature on the metabolism of ribo-and deoxyribonucleotides, nucleosides, and
nucleobases in Escherichia coli and Salmonella, including biosynthesis, degradation …

Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate …

JH Kim, JM Krahn, DR Tomchick, JL Smith… - Journal of Biological …, 1996 - ASBMB
Glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase from Escherichia coli
exhibits a basal PRPP-independent glutaminase activity having ak cat/K m that is 0.3% of …

A cysteine-histidine-aspartate catalytic triad is involved in glutamine amide transfer function in purF-type glutamine amidotransferases

B Mei, H Zalkin - Journal of Biological Chemistry, 1989 - ASBMB
A family of four glutamine amidotransferases has a homologous glutamine amide transfer
domain, designated purF-type, that is named after purF-encoded glutamine …

Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli

CRA Muchmore, JM Krahn, JL Smith, JH Kim… - Protein …, 1998 - Wiley Online Library
Crystal structures of glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase
from Escherichia coli have been determined to 2.0‐Å resolution in the absence of ligands …

The CBS subdomain of inosine 5′‐monophosphate dehydrogenase regulates purine nucleotide turnover

M Pimkin, GD Markham - Molecular microbiology, 2008 - Wiley Online Library
Summary Inosine 5′‐monophosphate dehydrogenase (IMPDH) catalyses the rate‐limiting
step in guanine nucleotide biosynthesis. IMPDH has an evolutionary conserved CBS …

A possible nucleotide-binding domain in the tertiary fold of phosphoribosyltransferases.

P Argos, M Hanei, JM Wilson, WN Kelley - Journal of Biological Chemistry, 1983 - ASBMB
Comparison of the primary structures of three phosphoribosyltransferases (human
hypoxanthine-guanine, Salmonella typhimurium ATP, and Escherichia coli glutamine) …

Glutamine PRPP amidotransferase: snapshots of an enzyme in action

JL Smith - Current opinion in structural biology, 1998 - Elsevier
Recent studies of glutamine PRPP amidotransferase have provided a new understanding of
the function and mechanism of this rather complicated enzyme that may be a paradigm for …