Applicability of glutaminyl-tRNA cyclotransferase in the peptide synthesis

1985 ◽  
Vol 50 (10) ◽  
pp. 2310-2318 ◽  
Author(s):  
Václav Čeřovský ◽  
Karel Jošt
Keyword(s):  
Glutamic Acid ◽  
Peptide Synthesis ◽  
Pyroglutamic Acid ◽  
Amino Terminal

Peptides with amino-terminal glutamine and their derivatives on treatment with crude papain preparation, containing glutaminyl-tRNA cyclotransferase (E.C. 2.3.2.5.), are converted into the corresponding compounds with pyroglutamic acid. This enzymic cyclization does not take place with glutamic acid or its γ-derivatives. The reaction has been optimized for the preparation of pyroglutamic acid phenylhydrazide. Glutaminyl-leucine phenylhydrazide and glutaminyl-histidyl-proline amide reacted to give pyroglutamyl-leucine phenylhydrazide and TRH, respectively. Treatment of crude papain with iodoacetamide completely inhibited its activity without affecting the glutaminyl-cyclotransferase activity.

Recombinant Production of Isotope-Labeled Peptides and Spontaneous Cyclization of Amino-Terminal Glutamine into Pyroglutamic Acid

ChemBioChem ◽  
2012 ◽  
Vol 13 (10) ◽  
pp. 1421-1423 ◽  
Author(s):  
André Mischo ◽  
Oliver Ohlenschläger ◽  
Karl-Heinz Gührs ◽  
Matthias Görlach
Keyword(s):  
Pyroglutamic Acid ◽  
Amino Terminal ◽  
Recombinant Production

Thermal-induced transformation of glutamic acid to pyroglutamic acid and self-cocrystallization: a charge–density analysis

2022 ◽  
Vol 78 (2) ◽  
Author(s):  
Sehrish Akram ◽  
Arshad Mehmood ◽  
Sajida Noureen ◽  
Maqsood Ahmed
Keyword(s):  
Hydrogen Bonds ◽  
Glutamic Acid ◽  
Single Crystal ◽  
Diffraction Data ◽  
Density Functional ◽  
Quantitative Estimation ◽  
Topological Analysis ◽  
Pyroglutamic Acid ◽  
X Ray Diffraction ◽  
X Ray

Thermal-induced transformation of glutamic acid to pyroglutamic acid is well known. However, confusion remains over the exact temperature at which this happens. Moreover, no diffraction data are available to support the transition. In this article, we make a systematic investigation involving thermal analysis, hot-stage microscopy and single-crystal X-ray diffraction to study a one-pot thermal transition of glutamic acid to pyroglutamic acid and subsequent self-cocrystallization between the product (hydrated pyroglutamic acid) and the unreacted precursor (glutamic acid). The melt upon cooling gave a robust cocrystal, namely, glutamic acid–pyroglutamic acid–water (1/1/1), C5H7NO3·C5H9NO4·H2O, whose structure has been elucidated from single-crystal X-ray diffraction data collected at room temperature. A three-dimensional network of strong hydrogen bonds has been found. A Hirshfeld surface analysis was carried out to make a quantitative estimation of the intermolecular interactions. In order to gain insight into the strength and stability of the cocrystal, the transferability principle was utilized to make a topological analysis and to study the electron-density-derived properties. The transferred model has been found to be superior to the classical independent atom model (IAM). The experimental results have been compared with results from a multipolar refinement carried out using theoretical structure factors generated from density functional theory (DFT) calculations. Very strong classical hydrogen bonds drive the cocrystallization and lend stability to the resulting cocrystal. Important conclusions have been drawn about this transition.

Synthesis of biobased succinimide from glutamic acid via silver-catalyzed decarboxylation

RSC Advances ◽  
2014 ◽  
Vol 4 (52) ◽  
pp. 27541-27544 ◽  
Author(s):  
Jin Deng ◽  
Qiu-Ge Zhang ◽  
Tao Pan ◽  
Qing Xu ◽  
Qing-Xiang Guo ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Pyroglutamic Acid ◽  
Oxidative Decarboxylation ◽  
Silver Catalyst ◽  
Step Procedure

Glutamic acid was transformed into succinimide in a two step procedure involving a dehydration in water to pyroglutamic acid followed by an oxidative decarboxylation using a silver catalyst.

STUDIES ON THE INHIBITION OF GLUTAMIC ACID UTILIZATION IN LACTOBACILLUS PLANTARUM

1962 ◽  
Vol 8 (6) ◽  
pp. 869-873 ◽  
Author(s):  
W. A. Zygmunt ◽  
R. L. Evans ◽  
Homer E. Stavely
Keyword(s):  
Glutamic Acid ◽  
Lactobacillus Plantarum ◽  
Bacterial Growth ◽  
Pyroglutamic Acid ◽  
Inhibition Of Growth ◽  
Acid Antagonist

Eighteen compounds including five novel γ-substituted glutamic acid analogues were tested for inhibition of the utilization of L-glutamic acid by Lactobacillus plantarum. All of the test compounds were found to be less active than DL-methionine sulphoxide, a known glutamic acid antagonist, in inhibiting" the growth of L. plantarum. γ-Methylene-DL-glutamic acid and N-benzyl-α-methyl-DL-pyroglutamic acid were found to be the most active inhibitors of bacterial growth. The inhibition of growth produced by γ-methylene-DL-glutamic acid was readily reversed by L-glutamic acid; whereas the inhibition caused by α-methyl-DL-pyroglutamic acid was more refractory to reversal by L-glutamic acid.

Metabolism of 14C-Labeled Glutamic Acid and Pyroglutamic Acid in Animals

1966 ◽  
Vol 55 (10) ◽  
pp. 1147-1149 ◽  
Author(s):  
Winthrop E. Lange ◽  
Edward F. Carey
Keyword(s):  
Glutamic Acid ◽  
Pyroglutamic Acid

scholarly journals Characterization of Bacteriophage Lambda Excisionase Mutants Defective in DNA Binding

2000 ◽  
Vol 182 (20) ◽  
pp. 5807-5812 ◽  
Author(s):  
Eun Hee Cho ◽  
Renato Alcaraz ◽  
Richard I. Gumport ◽  
Jeffrey F. Gardner
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Glutamic Acid ◽  
Cooperative Interaction ◽  
Mutant Proteins ◽  
Amino Terminal ◽  
Factor For Inversion Stimulation ◽  
Α Helix

ABSTRACT The bacteriophage λ excisionase (Xis) is a sequence-specific DNA binding protein required for excisive recombination. Xis binds cooperatively to two DNA sites arranged as direct repeats on the phage DNA. Efficient excision is achieved through a cooperative interaction between Xis and the host-encoded factor for inversion stimulation as well as a cooperative interaction between Xis and integrase. The secondary structure of the Xis protein was predicted to contain a typical amphipathic helix that spans residues 18 to 28. Several mutants, defective in promoting excision in vivo, were isolated with mutations at positions encoding polar amino acids in the putative helix (T. E. Numrych, R. I. Gumport, and J. F. Gardner, EMBO J. 11:3797–3806, 1992). We substituted alanines for the polar amino acids in this region. Mutant proteins with substitutions for polar amino acids in the amino-terminal region of the putative helix exhibited decreased excision in vivo and were defective in DNA binding. In addition, an alanine substitution at glutamic acid 40 also resulted in altered DNA binding. This indicates that the hydrophilic face of the α-helix and the region containing glutamic acid 40 may form the DNA binding surfaces of the Xis protein.

Sign in / Sign up

Export Citation Format

Share Document