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

Site-directed mutagenesis shows that tyrosine 248 of carboxypeptidase A does not play a crucial role in catalysis.

Nature - 1 Jan 2000

Gardell S J, Craik C S, Hilvert D, Urdea M S, Rutter W J

Abstract excerpt

The residue Tyr 248 of carboxypeptidase A (CPA) is thought to play a role in catalysis by contributing a proton to the incipient amine anion generated during cleavage of peptide substrates. To test this hypothesis we have modified the rat CPA cDNA by site-directed mutagenesis so that the codon fo...

Topics

Amino Acid Sequence
Animals
Base Sequence
Carboxypeptidases
Carboxypeptidases A
DNA
Hydrolysis
Kinetics
Mutation
Phenylalanine
Rats
Tyrosine
X-Ray Diffraction

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Yeasts

Source

Identifiers

PMID: 3840231
DOI: 10.1038/317551a0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-3840231-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Site-directed mutagenesis shows that tyrosine 248 of carboxypeptidase A does not play a crucial role in catalysis.PMID 3840231Read ↗

Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids.Semantic proximity Read ↗

Delineation of the catalytic core of phenylalanine hydroxylase and identification of glutamate 286 as a critical residue for pterin function.Semantic proximity Read ↗

Purification and characterization of S1 mutants of alpha-lytic protease having altered catalytic properties.Semantic proximity Read ↗

A tobacco etch virus protease with increased substrate tolerance at the P1' position.Semantic proximity Read ↗

Random substitution of large parts of the propeptide of yeast proteinase A.Semantic proximity Read ↗

Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.Semantic proximity Read ↗

Characterization of recombinant rat cathepsin B and nonglycosylated mutants expressed in yeast. New insights into the pH dependence of cathepsin B-catalyzed hydrolyses.Semantic proximity Read ↗

Identification of critical residues in the active site of porcine membrane-bound aminopeptidase P.Semantic proximity Read ↗

Investigation of the role of a second conserved serine in carboxylesterases via site-directed mutagenesis.Semantic proximity Read ↗

A conserved tyrosine residue of Saccharomyces cerevisiae leukotriene A4 hydrolase stabilizes the transition state of the peptidase activity.Semantic proximity Read ↗

The propeptide is required for in vivo formation of stable active yeast proteinase A and can function even when not covalently linked to the mature region.Semantic proximity Read ↗

Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility.Semantic proximity Read ↗

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