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

Identification of the active site serine in pancreatic cholesterol esterase by chemical modification and site-specific mutagenesis.

The Journal of biological chemistry - 5 Oct 1990

DiPersio L P, Fontaine R N, Hui D Y

Abstract excerpt

Chemical modification and site-specific mutagenesis approaches were used in this study to identify the active site serine residue of pancreatic cholesterol esterase. In the first approach, purified porcine pancreatic cholesterol esterase was covalently modified by incubation with [3H]diisopropylfluorophosphate (DFP). The radiolabeled cholesterol esterase was digested with CNBr, and the peptides were separated by...

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 Base Sequence
Share to Binding Sites

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

Share to Kinetics

Share to Molecular Sequence Data

Share to Mutation

Share to Oligonucleotide Probes

Share to Peptide Fragments

Source

Identifiers

PMID: 2211595

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

Identification of the active site serine in pancreatic cholesterol esterase by chemical modification and site-specific mutagenesis.PMID 2211595Read ↗

Identification of two serine residues involved in catalysis by fatty acid amide hydrolase.Semantic proximity Read ↗

Structural and functional roles of highly conserved serines in human lipoprotein lipase. Evidence that serine 132 is essential for enzyme catalysis.Semantic proximity Read ↗

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

Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase.Semantic proximity Read ↗

Mutagenesis of essential functional residues in acetylcholinesterase.Semantic proximity Read ↗

Utilization of an active serine 101----cysteine mutant to demonstrate the proximity of the catalytic serine 101 and histidine 237 residues in thioesterase II.Semantic proximity Read ↗

Study of arachidonoyl specificity in two enzymes of the PI cycle.Semantic proximity Read ↗

Reengineering the specificity of a serine active-site enzyme. Two active-site mutations convert a hydrolase to a transferase.Semantic proximity Read ↗

Guinea pig phospholipase B, identification of the catalytic serine and the proregion involved in its processing and enzymatic activity.Semantic proximity Read ↗

Isolation of cholesterol-requiring mutant Chinese hamster ovary cells with defects in cleavage of sterol regulatory element-binding proteins at site 1.Semantic proximity Read ↗

Identification of the catalytic residues of carboxylesterase from Arthrobacter globiformis by diisopropyl fluorophosphate-labeling and site-directed mutagenesis.Semantic proximity Read ↗

Identification of residues involved in v-Src substrate recognition by site-directed mutagenesis.Semantic proximity Read ↗

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