Pancreatic lipase structure-function relationships by domain exchange.

doi:10.1021/bi961991p

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Article

Pancreatic lipase structure-function relationships by domain exchange.

Biochemistry - 7 Jan 1997

Carrière F, Thirstrup K, Hjorth S, Ferrato F, Nielsen P F, Withers-Martinez C, Cambillau C, Boel E, Thim L, Verger R

Abstract excerpt

We designed chimeric mutants by exchanging the lid domains of the classical human pancreatic lipase (HPL) and the guinea pig pancreatic lipase related protein 2 (GPLRP2). This latter enzyme possesses naturally a large deletion within the lid domain and is not activated by lipid/water interfaces....

Topics

Amino Acid Sequence
Animals
Base Sequence
Bile Acids and Salts
Colipases
DNA Primers
Enzyme Activation
Glycosylation
Guinea Pigs
Humans
Lipase
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Pancreas
Phospholipids
Recombinant Fusion Proteins
Sequence Analysis

Source

Open in PubMed

Identifiers

PMID: 8993339
DOI: 10.1021/bi961991p

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8993339-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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