scholarly journals Substrate specificity of l-δ-(α-aminoadipoyl)-l-cysteinyl-d-valine synthetase from Cephalosporium acremonium: demonstration of the structure of several unnatural tripeptide products

1994 ◽  
Vol 301 (2) ◽  
pp. 367-372 ◽  
Author(s):  
J E Baldwin ◽  
C Y Shiau ◽  
M F Byford ◽  
C J Schofield
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Substrate Specificity ◽  
Electrospray Ionization ◽  
Peptide Synthesis ◽  
Thiol Group ◽  
Cephalosporium Acremonium ◽  
Peptide Synthetases ◽  
Peptide Formation ◽  
Combined Use

Potential substrates for L-delta-(alpha-aminoadipoyl)-L-(cysteinyl)-D-valine (ACV) synthetase were initially identified using both the amino-acid-dependent ATP<-->pyrophosphate exchange reaction catalysed by the enzyme and the incorporation of 14C-radiolabelled cysteine and valine into potential peptide products. S-Carboxymethylcysteine was an effective substitute for alpha-aminoadipate and both allylglycine and vinylglycine could substitute for cysteine, indicating that the thiol group of cysteine is not essential for peptide formation. L-allo-Isoleucine but not L-isoleucine substituted effectively for valine. The structures of the presumed peptide products derived from these amino acids were confirmed by combined use of electrospray-ionization m.s. (e.s.m.s.) and 1H n.m.r. These results clearly indicate that, in common with other peptide synthetases, but in contrast with ribosomal peptide synthesis, ACV synthetase has a relatively broad substrate specificity.

Fmoc amino acid fluorides in peptide synthesis — Extension of the method to extremely hindered amino acids

1996 ◽  
Vol 37 (31) ◽  
pp. 5483-5486 ◽  
Author(s):  
Holger Wenschuh ◽  
Michael Beyermann ◽  
Rüdiger Winter ◽  
Michael Bienert ◽  
Dumitru Ionescu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Peptide Synthesis ◽  
Amino Acid Fluorides ◽  
Acid Fluorides

scholarly journals Incorporation of 3H from δ-(l-α-amino (4,5-3H)adipyl)-l-cysteinyl-d-(4,4-3H)valine into isopenicillin N

1979 ◽  
Vol 184 (2) ◽  
pp. 421-426 ◽  
Author(s):  
J O'Sullivan ◽  
R C Bleaney ◽  
J A Huddleston ◽  
E P Abraham
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Adipic Acid ◽  
Experimental Error ◽  
Acid Oxidase ◽  
Cephalosporium Acremonium ◽  
Amino Acid Oxidase ◽  
Free System ◽  
A Cell ◽  
Isopenicillin N

1. delta-(L-alpha-Amino[4,5-3H]adipyl)-L-cysteinyl-D-[4,4-3H]valine has been synthesized from its constituent amino acids, the L-alpha-amino[4,5-3H]adipic acid being obtained by reduction with 3H2 of methyl 5-acetamido-5,5-diethoxycarbonylpent-2-enoate and subsequent decarboxylation and hydrolysis. 2. In a cell-free system prepared by lysis of protoplasts of Cephalosporium acremonium 3H was incorporated from the doubly labelled tripeptide into a compound that behaved like penicillin N or isopenicillin N. The relative specific radioactivities of the alpha-aminoadipyl and penicillamine moieties of the penicillin were the same (within experimental error) as those of the alpha-aminoadipic acid and valine residues respectively of the tripeptide. 3. The behaviour of the labelled alpha-aminoadipic acid from the penicillin to the L-amino acid oxidase of Crotalus adamanteus venom showed that it was mainly L-alpha-aminoadipic acid. 4. The results are consistent with the hypothesis that the carbon skeleton of the LLD-tripeptide is incorporated intact into the penicillin molecule and that the first product is isopenicillin N.

N-Methylamino acids in peptide synthesis. V. The synthesis of N-tert-butyloxycarbonyl, N-methylamino acids by N-methylation

1977 ◽  
Vol 55 (5) ◽  
pp. 906-910 ◽  
Author(s):  
S. T. Cheung ◽  
N. Leo Benoiton
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Methyl Iodide ◽  
Peptide Synthesis ◽  
Room Temperature ◽  
Sodium Hydride ◽  
Amino Acid Derivatives ◽  
Enantiomerically Pure ◽  
Neutral Amino Acids ◽  
Related Data

The preparation of enantiomerically pure N-tert-butyloxycarbonyl,N-methylamino acids by N-methylation of the parent amino acid derivatives using sodium hydride and methyl iodide in tetrahydrofuran at room temperature is described for neutral amino acids including O-benzyl-protected threonine and tyrosine. Methylation of the O-benzylserine derivative under these conditions gives the N-methyldehydroalanine derivative. The β-elimination is completely suppressed, giving the corresponding N-methylserine derivative when the reaction is carried out at 5 °C. Other related data on N-methylation and N-methylamino acid derivatives are presented.

scholarly journals Size does matter: 18 amino acids at the N-terminal tip of an amino acid transporter in Leishmania determine substrate specificity

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Doreen Schlisselberg ◽  
Eldar Mazarib ◽  
Ehud Inbar ◽  
Doris Rentsch ◽  
Peter J. Myler ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Substrate Specificity ◽  
Amino Acid Transporter ◽  
Acid Transporter

scholarly journals Enzymic synthesis of N-acetyl-l-phenylalanine in Escherichia coli K12

1971 ◽  
Vol 124 (5) ◽  
pp. 905-913 ◽  
Author(s):  
R. V. Krishna ◽  
P. R. Krishnaswamy ◽  
D. Rajagopal Rao
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Amino Acid ◽  
Substrate Specificity ◽  
Acetyl Coa ◽  
Ph Optimum ◽  
E Coli ◽  
Enzymic Synthesis ◽  
Escherichia Coli K12

1. Cell-free extracts of Escherichia coli K12 catalyse the synthesis of N-acetyl-l-phenylalanine from acetyl-CoA and l-phenylalanine. 2. The acetyl-CoA–l-phenylalanine α-N-acetyltransferase was purified 160-fold from cell-free extracts. 3. The enzyme has a pH optimum of 8 and catalyses the acetylation of l-phenylalanine. Other l-amino acids such as histidine and alanine are acetylated at slower rates. 4. A transacylase was also purified from E. coli extracts and its substrate specificity studied. 5. The properties of both these enzymes were compared with those of other known amino acid acetyltransferases and transacylases.

scholarly journals A GC-MS/Single-Cell Method to Evaluate Membrane Transporter Substrate Specificity and Signaling

2021 ◽  
Vol 8 ◽  
Author(s):  
Stephen J. Fairweather ◽  
Shoko Okada ◽  
Gregory Gauthier-Coles ◽  
Kiran Javed ◽  
Angelika Bröer ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Substrate Specificity ◽  
Signaling Pathways ◽  
Intracellular Signaling ◽  
Vital Role ◽  
Cellular Growth ◽  
Amino Acid Transporters ◽  
Cationic Amino Acids ◽  
Nutrient Signaling

Amino acid transporters play a vital role in metabolism and nutrient signaling pathways. Typically, transport activity is investigated using single substrates and competing amounts of other amino acids. We used GC-MS and LC-MS for metabolic screening of Xenopus laevis oocytes expressing various human amino acid transporters incubated in complex media to establish their comprehensive substrate profiles. For most transporters, amino acid selectivity matched reported substrate profiles. However, we could not detect substantial accumulation of cationic amino acids by SNAT4 and ATB0,+ in contrast to previous reports. In addition, comparative substrate profiles of two related sodium neutral amino acid transporters known as SNAT1 and SNAT2, revealed the latter as a significant leucine accumulator. As a consequence, SNAT2, but not SNAT1, was shown to be an effective activator of the eukaryotic cellular growth regulator mTORC1. We propose, that metabolomic profiling of membrane transporters in Xenopus laevis oocytes can be used to test their substrate specificity and role in intracellular signaling pathways.

scholarly journals The Rare Amino Acid Building Block 3-(3-furyl)-Alanine in the Formation of Non-ribosomal Peptides

2017 ◽  
Vol 12 (1) ◽  
pp. 1934578X1701200 ◽  
Author(s):  
Fayrouz El Maddah ◽  
Mamona Nazir ◽  
Gabriele M. König
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Secondary Metabolites ◽  
Cyclosporine A ◽  
Building Block ◽  
Therapeutic Potential ◽  
Rhizopus Microsporus ◽  
Bacterial Endosymbiont ◽  
Peptide Synthetases ◽  
Microbial Origin

Microorganisms have made considerable contributions to the production of peptide secondary metabolites, many of them with therapeutic potential, e.g., the fungus-derived immunosuppressant cyclosporine A and the antibiotic daptomycin originating from Streptomyces. Most of the medically used peptides are the product of non-ribosomal peptide synthetases (NRPS), incorporating apart from proteinogenic also unique, non-proteinogenic amino acids into the peptides. An extremely rare such amino acid is 3-(3-furyl)-alanine. So far, only few peptides have been found that contain this residue, including the rhizonins, bingchamide B and endolides. The producer of the rhizonins was proven to be the bacterial endosymbiont Burkholderia endofungorum inside the fungus Rhizopus microsporus. The microbial origin, chemistry and bioactivity of the 3-(3-furyl)-alanine containing peptides are the focus of this review.

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