The acid/base catalyst in the exoglucanase/xylanase from Cellulomonas fimi is glutamic acid 127: evidence from detailed kinetic studies of mutants.

doi:10.1021/bi00186a042

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

The acid/base catalyst in the exoglucanase/xylanase from Cellulomonas fimi is glutamic acid 127: evidence from detailed kinetic studies of mutants.

Biochemistry - 24 May 1994

MacLeod A M, Lindhorst T, Withers S G, Warren R A

Abstract excerpt

The exoglucanase/xylanase Cex from Cellulomonas fimi hydrolyzes beta-1,4-glycosidic bonds with net retention of anomeric configuration, releasing the disaccharides beta-cellobiose or beta-xylobiose. It uses a double-displacement mechanism involving a glycosyl-enzyme intermediate which is formed a...

Topics

Actinomycetales
Amino Acid Sequence
Azides
Base Sequence
Catalysis
Cellobiose
Cloning, Molecular
Disaccharides
Escherichia coli
Glucan 1,4-beta-Glucosidase
Glutamates
Glutamic Acid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Glycosylation

Hydrogen-Ion Concentration

Kinetics

Molecular Sequence Data

Mutagenesis, Site-Directed

Mutation

Source

Open in PubMed

Identifiers

PMID: 7910761
DOI: 10.1021/bi00186a042

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7910761-2026-08-30.1. 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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The acid/base catalyst in the exoglucanase/xylanase from Cellulomonas fimi is glutamic acid 127: evidence from detailed kinetic studies of mutants.PMID 7910761Read ↗

Mechanistic consequences of mutation of active site carboxylates in a retaining beta-1,4-glycanase from Cellulomonas fimi.Semantic proximity Read ↗

Positioning the acid/base catalyst in a glycosidase: studies with Bacillus circulans xylanase.Semantic proximity Read ↗

Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism.Semantic proximity Read ↗

Structural and biochemical characterization of glycoside hydrolase family 79 β-glucuronidase from Acidobacterium capsulatum.Semantic proximity Read ↗

Transglycosylation Activity of Catalytic Domain Mutant of Endo-1,3-β-glucanase from Cellulosimicrobium cellulans.Semantic proximity Read ↗

Paenibacillus sp. TS12 glucosylceramidase: kinetic studies of a novel sub-family of family 3 glycosidases and identification of the catalytic residues.Semantic proximity Read ↗

Probing the catalytically essential residues of the alpha-L-arabinofuranosidase from Thermobacillus xylanilyticus.Semantic proximity Read ↗

Structural basis for transglycosylation in glycoside hydrolase family GH116 glycosynthases.Semantic proximity Read ↗

A transitional hydrolase to glycosynthase mutant by Glu to Asp substitution at the catalytic nucleophile in a retaining glycosidase.Semantic proximity Read ↗

Modulating the pH-activity profile of cellulase A from Cellulomonas fimi by replacement of surface residues.Semantic proximity Read ↗

Biochemical identification of the catalytic residues of a glycoside hydrolase family 120 β-xylosidase, involved in xylooligosaccharide metabolisation by gut bacteria.Semantic proximity Read ↗

Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural analysis of covalent reaction intermediates.Semantic proximity Read ↗

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