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

Structure-function relationships in naturally occurring mutants of pancreatic lipase.

Protein engineering - 1 Apr 1994

Carrière F, Thirstrup K, Boel E, Verger R, Thim L

Abstract excerpt

From primary structure comparison, the pancreatic lipase family is now divided into three subgroups: classical pancreatic lipases, pancreatic lipase-related proteins 1 (RPI) and pancreatic lipase-related proteins 2 (RP2). Among the RP2 subfamily, the guinea-pig and coypu enzymes share kinetic properties which differ from those of classical pancreatic lipases. Both enzymes display a high phospholipase activity and...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Enzyme Activation
Share to Models, Biological

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

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Mutation

Share to Recombinant Proteins

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 8029213
DOI: 10.1093/protein/7.4.563

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

Structure-function relationships in naturally occurring mutants of pancreatic lipase.PMID 8029213Read ↗

Pancreatic lipase structure-function relationships by domain exchange.Semantic proximity Read ↗

A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig.Semantic proximity Read ↗

An inactive pancreatic lipase-related protein is activated into a triglyceride-lipase by mutagenesis based on the 3-D structure.Semantic proximity Read ↗

Cloning of the classical guinea pig pancreatic lipase and comparison with the lipase related protein 2Semantic proximity Read ↗

Identification of a novel mutation in the PNLIP gene in two brothers with congenital pancreatic lipase deficiency.Semantic proximity Read ↗

Missense PNLIP mutations impeding pancreatic lipase secretion cause protein misfolding and endoplasmic reticulum stress.Semantic proximity Read ↗

Functional predictors of pathogenicity of missense CPA1 variants in chronic pancreatitisSemantic proximity Read ↗

Molecular and functional diversity of yeast and fungal lipases: their role in biotechnology and cellular physiology.Semantic proximity Read ↗

Recurrent pancreatitis and chylomicronemia in an extended Dutch kindred is caused by a Gly154-->Ser substitution in lipoprotein lipase.Semantic proximity Read ↗

Role of the lid hydrophobicity pattern in pancreatic lipase activity.Semantic proximity Read ↗

Val-407 and Ile-408 in the beta5'-loop of pancreatic lipase mediate lipase-colipase interactions in the presence of bile salt micelles.Semantic proximity Read ↗

Single nucleotide polymorphisms in CEL-HYB1 increase risk for chronic pancreatitis through proteotoxic misfolding.Semantic proximity Read ↗

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