Conversion of protein farnesyltransferase to a geranylgeranyltransferase.

doi:10.1021/bi060295e

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

Back to search

Article

Conversion of protein farnesyltransferase to a geranylgeranyltransferase.

Biochemistry - 15 Aug 2006

Terry Kimberly L, Casey Patrick J, Beese Lorena S

Abstract excerpt

Posttranslational modifications are essential for the proper function of a number of proteins in the cell. One such modification, the covalent attachment of a single isoprenoid lipid (prenylation), is carried out by the CaaX prenyltransferases, protein farnesyltransferase (FTase) and protein geranylgeranyltransferase type-I (GGTase-I). Substrate proteins of these two enzymes are involved in a variety of cellular...

Topics

Alkyl and Aryl Transferases
Binding Sites
Crystallography, X-Ray
Farnesyltranstransferase
Humans
Models, Molecular
Mutation
Peptides
Protein Prenylation
Substrate Specificity

Source

Open in PubMed

Identifiers

PMID: 16893176
DOI: 10.1021/bi060295e

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics