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

Role of carbohydrate moiety in carboxypeptidase Y: structural study of mutant enzyme lacking carbohydrate moiety.

Bioscience, biotechnology, and biochemistry - 1 Jun 1999

Shimizu H, Ueno H, Hayashi R

Abstract excerpt

To study the roles of the carbohydrate moiety in the function of carboxypeptidase Y, asparagine residues at 13, 87, 168, and 368, the four-consensus N-linked glycosylation sites, were altered to alanine with site-directed mutagenesis. The mutant enzyme of 51 kDa completely lost the carbohydrate moiety which was present in the 61-kDa wild-type enzyme. Structural studies of the mutant enzyme showed that it...

Read the complete abstract on PubMed

Topics

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

Share to Carbohydrates
Share to Carboxypeptidases
Share to Cathepsin A

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Weight

Share to Mutagenesis, Site-Directed

Share to Plasmids

Share to Protein Conformation

Share to Protein Denaturation

Source

Identifiers

PMID: 10427689
DOI: 10.1271/bbb.63.1045

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of carbohydrate moiety in carboxypeptidase Y: structural study of mutant enzyme lacking carbohydrate moiety.PMID 10427689Read ↗

Role of N-glycosylation in cathepsin E. A comparative study of cathepsin E with distinct N-linked oligosaccharides and its nonglycosylated mutant.Semantic proximity Read ↗

Glu88 in the non-catalytic domain of acylpeptide hydrolase plays dual roles: charge neutralization for enzymatic activity and formation of salt bridge for thermodynamic stability.Semantic proximity Read ↗

Evaluation of chitosan-binding amino acid residues of chitosanase from Paenibacillus fukuinensis.Semantic proximity Read ↗

Gradually glycosylated protein C mutants (Arg178Gln and Cys331Arg) are degraded by proteasome after mannose trimming.Semantic proximity Read ↗

Increased proteolytic susceptibility of carboxypeptidase Y caused by modification of the disulfide zipper.Semantic proximity Read ↗

The flexibility of the non-conservative region at the C terminus of D-hydantoinase from Pseudomonas putida YZ-26 is extremely limited.Semantic proximity Read ↗

Structure of a bacterial glycoside hydrolase family 63 enzyme in complex with its glycosynthase product, and insights into the substrate specificity.Semantic proximity Read ↗

Crystal structure of a mutant glycosylasparaginase shedding light on aspartylglycosaminuria-causing mechanism as well as on hydrolysis of non-chitobiose substrate.Semantic proximity Read ↗

Improvement of thermostability and halostability of β-1,3-1,4-glucanase by substituting hydrophobic residue for Lys48.Semantic proximity Read ↗

Yeast carboxypeptidase Y requires glycosylation for efficient intracellular transport, but not for vacuolar sorting, in vivo stability, or activity.Semantic proximity Read ↗

Contribution of Ser463 residue to the enzymatic and autoprocessing activities of Escherichia coli gamma-glutamyltranspeptidase.Semantic proximity Read ↗

Deletion analysis of regions at the C-terminal part of cycloisomaltooligosaccharide glucanotransferase from Bacillus circulans T-3040.Semantic proximity Read ↗

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