L
Larry Reitzer
Researcher at University of Texas at Dallas
Publications - 57
Citations - 5041
Larry Reitzer is an academic researcher from University of Texas at Dallas. The author has contributed to research in topics: Escherichia coli & Operon. The author has an hindex of 32, co-authored 49 publications receiving 4737 citations. Previous affiliations of Larry Reitzer include Massachusetts Institute of Technology & Washington University in St. Louis.
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Journal ArticleDOI
The redundant aminotransferases in lysine and arginine synthesis and the extent of aminotransferase redundancy in Escherichia coli.
TL;DR: Complementation analysis of mutants lacking aminotransferases showed that the SDAP‐ATs and alanine aminotsferases were exceptionally redundant, and it is proposed that this redundancy may ensure peptidoglycan synthesis.
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Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli.
Ante Tocilj,Joseph D. Schrag,Yunge Li,Barbara L. Schneider,Larry Reitzer,Allan Matte,Miroslaw Cygler +6 more
TL;DR: The crystal structure of N-succinylarginine dihydrolase AstB, the second enzyme of the arginine succinyltransferase pathway, is reported, providing the first structural insight into enzymes from this pathway.
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Phosphorylation-independent dimer-dimer interactions by the enhancer-binding activator NtrC of Escherichia coli: A third function for the C-terminal domain
TL;DR: In this paper, the structural determinants and function of this central domain independent as well as phosphorylation-independent oligomerization were analyzed and mutagenized DNA coding for an NtrC without its central domain.
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Effects of insertions and deletions in glnG (ntrC) of Escherichia coli on nitrogen regulator I-dependent DNA binding and transcriptional activation.
TL;DR: The results suggest that the 70 amino acids from residue 400 to the carboxyl terminus constitute a DNA-binding domain that includes residues for specific contacts and dimerization and suggest that transcription from glnAp2 without specific NRI-binding sites requires binding to sites with some similarity to the specific sites.
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Salmonella typhimurium nit Is nadE: Defective Nitrogen Utilization and Ammonia-Dependent NAD Synthetase
TL;DR: Evidence is presented that ammonia, not glutamine, is the physiological substrate for eubacterial NAD synthetases and that low activity completely accounts for the mutant phenotype of typhimurium nit mutants.