Constructing tailored isoprenoid products by structure-guided modification of geranylgeranyl reductase.

doi:10.1016/j.str.2014.05.007

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

Constructing tailored isoprenoid products by structure-guided modification of geranylgeranyl reductase.

Structure (London, England : 1993) - 8 Jul 2014

Kung Yan, McAndrew Ryan P, Xie Xinkai, Liu Charlie C, Pereira Jose H, Adams Paul D, Keasling Jay D

Abstract excerpt

The archaeal enzyme geranylgeranyl reductase (GGR) catalyzes hydrogenation of carbon-carbon double bonds to produce the saturated alkyl chains of the organism's unusual isoprenoid-derived cell membrane. Enzymatic reduction of isoprenoid double bonds is of considerable interest both to natural products researchers and to synthetic biologists interested in the microbial production of isoprenoid drug or biofuel...

Topics

Archaeal Proteins
Crystallography, X-Ray
Kinetics
Models, Molecular
Molecular Structure
Mutation
Oxidoreductases
Polyisoprenyl Phosphates
Protein Binding
Protein Structure, Tertiary
Substrate Specificity
Sulfolobus acidocaldarius
Terpenes

Source

Open in PubMed

Identifiers

PMID: 24954619
DOI: 10.1016/j.str.2014.05.007

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 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