Determination of the roles of Glu-461 in beta-galactosidase (Escherichia coli) using site-specific mutagenesis.

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

Determination of the roles of Glu-461 in beta-galactosidase (Escherichia coli) using site-specific mutagenesis.

The Journal of biological chemistry - 5 Apr 1990

Cupples C G, Miller J H, Huber R E

Abstract excerpt

Site-directed substitutions (Asp, Gly, Gln, His, and Lys) were made for Glu-461 of beta-galactosidase (Escherichia coli). All substitutions resulted in loss of most activity. Substrates and a substrate analog inhibitor were bound better by the Asp-substituted enzyme than by the normal enzyme, abo...

Topics

Binding Sites
Drug Stability
Edetic Acid
Escherichia coli
Galactosidases
Glutamates
Glutamic Acid
Hydrogen-Ion Concentration
Kinetics
Lactose
Mutation
Nitrophenylgalactosides
Ribose
Structure-Activity Relationship
beta-Galactosidase

Source

Open in PubMed

Identifiers

PMID: 1969405

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1969405-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 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