Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Guanidine derivatives restore activity to carboxypeptidase lacking arginine-127.

Protein science : a publication of the Protein Society - 1 Apr 1992

Phillips M A, Hedstrom L, Rutter W J

Abstract excerpt

Arg-127 stabilizes the oxyanion of the tetrahedral intermediate formed during Zn2+ carboxypeptidase A-catalyzed hydrolysis. Mutant carboxypeptidases lacking Arg-127 exhibit substantially reduced rates of hydrolysis with the change manifest almost entirely in kcat (kcat/Km is decreased by 10(4) for R127A). Therefore, Arg-127 stabilizes the enzyme-transition state complex but not the ground state enzyme-substrate...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Arginine
Share to Carboxypeptidases
Share to Guanidine

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Guanidines

Share to Mutation

Share to Peptides

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 1304353
DOI: 10.1002/pro.5560010406
PMCID: PMC2142216

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Guanidine derivatives restore activity to carboxypeptidase lacking arginine-127.PMID 1304353Read ↗

Transition-state characterization: a new approach combining inhibitor analogues and variation in enzyme structure.Semantic proximity Read ↗

Kinetic studies and site-directed mutagenesis of Escherichia coli agmatinase. A role for Glu274 in binding and correct positioning of the substrate guanidinium group.Semantic proximity Read ↗

Noncoded amino acid replacement probes of the aspartate aminotransferase mechanism.Semantic proximity Read ↗

The Escherichia coli F1-ATPase mutant beta Tyr-297-->Cys: functional studies and asymmetry of the enzyme under various nucleotide conditions based on reaction of the introduced Cys with N-ethylmaleimide and 7-chloro-4-nitrobenzofurazan.Semantic proximity Read ↗

Re-examining the role of Lys67 in class C beta-lactamase catalysis.Semantic proximity Read ↗

Kinetic and thermodynamic consequences of the removal of the Cys-77-Cys-123 disulphide bond for the folding of TEM-1 beta-lactamase.Semantic proximity Read ↗

A positively charged amino acid at position 129 in nitrilase from Rhodococcus rhodochrous ATCC 33278 is an essential residue for the activity with meta-substituted benzonitriles.Semantic proximity Read ↗

Mutation of arginine 98, which serves as a substrate-recognition site of D-amino acid aminotransferase, can be partly compensated for by mutation of tyrosine 88 to an arginyl residue.Semantic proximity Read ↗

Mutations affecting transition-state stabilization by residues coordinating zinc at the active site of cytidine deaminase.Semantic proximity Read ↗

The role of the active site glutamate in the rearrangement of glutamate to 3-methylaspartate catalyzed by adenosylcobalamin-dependent glutamate mutase.Semantic proximity Read ↗

Chemical rescue and inhibition studies to determine the role of Arg301 in phosphite dehydrogenase.Semantic proximity Read ↗

Mutation of active site residues of the puromycin-sensitive aminopeptidase: conversion of the enzyme into a catalytically inactive binding protein.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.