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

Kinetic and structural evidences on human prolidase pathological mutants suggest strategies for enzyme functional rescue.

PloS one - 1 Jan 2013

Besio Roberta, Gioia Roberta, Cossu Federica, Monzani Enrico, Nicolis Stefania, Cucca Lucia, Profumo Antonella, Casella Luigi, Tenni Ruggero, Bolognesi Martino, Rossi Antonio, Forlino Antonella

Abstract excerpt

Prolidase is the only human enzyme responsible for the digestion of iminodipeptides containing proline or hydroxyproline at their C-terminal end, being a key player in extracellular matrix remodeling. Prolidase deficiency (PD) is an intractable loss of function disease, characterized by mutations in the prolidase gene. The exact causes of activity impairment in mutant prolidase are still unknown. We generated...

Read the complete abstract on PubMed

Topics

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

Share to Coenzymes
Share to Dipeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to Fibroblasts

Share to Heat-Shock Proteins

Share to Manganese

Share to Protein Multimerization

Share to Protein Structure, Quaternary

Source

Open in PubMed Open full text

Identifiers

PMID: 23516557
DOI: 10.1371/journal.pone.0058792
PMCID: PMC3596340

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Kinetic and structural evidences on human prolidase pathological mutants suggest strategies for enzyme functional rescue.PMID 23516557Read ↗

Human prolidase and prolidase deficiency: an overview on the characterization of the enzyme involved in proline recycling and on the effects of its mutations.Semantic proximity Read ↗

Structural basis for prolidase deficiency disease mechanisms.Semantic proximity Read ↗

Prolidase function in proline metabolism and its medical and biotechnological applicationsSemantic proximity Read ↗

Clinical Genetics of Prolidase Deficiency: An Updated ReviewSemantic proximity Read ↗

PROLIDASE: A Review from Discovery to its Role in Health and DiseaseSemantic proximity Read ↗

Harnessing natural diversity to identify key amino acid residues in prolidaseSemantic proximity Read ↗

Structure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunit.Semantic proximity Read ↗

Comprehensive in-silico prediction of damage associated SNPs in Human Prolidase gene.Semantic proximity Read ↗

Molecular characterisation of six patients with prolidase deficiency: identification of the first small duplication in the prolidase gene and of a mutation generating symptomatic and asymptomatic outcomes within the same family.Semantic proximity Read ↗

Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: insights into substrate recognition and the mechanism of catalysis.Semantic proximity Read ↗

Glutamate Carboxypeptidase II: An Overview of Structural Studies and Their Importance for Structure-Based Drug Design and Deciphering the Reaction Mechanism of the EnzymeSemantic proximity Read ↗

Characterization of a new PEPD allele causing prolidase deficiency in two unrelated patients: natural-occurrent mutations as a tool to investigate structure-function relationship.Semantic proximity Read ↗

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