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

Tyrosine residue 300 is important for activity and stability of branching enzyme from Escherichia coli.

Archives of biochemistry and biophysics - 15 Jan 2001

Mikkelsen R, Binderup K, Preiss J

Abstract excerpt

Branching enzyme belongs to the alpha-amylase family, which includes enzymes that catalyze hydrolysis or transglycosylation at alpha-(1,4)- or alpha-(1,6)-glucosidic linkages. In the alpha-amylase family, four highly conserved regions are proposed to make up the active site. From amino acid seque...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to 1,4-alpha-Glucan Branching Enzyme
Share to Amino Acid Substitution
Share to Catalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Conserved Sequence

Share to Enzyme Stability

Share to Hot Temperature

Share to Mutagenesis, Site-Directed

Share to Tyrosine

Source

Identifiers

PMID: 11368019
DOI: 10.1006/abbi.2000.2164

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026. Prepared record publication-11368019-2026-08-31.1. Manifest publication-graph-cohort-2026-08-31.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 31 Aug 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Tyrosine residue 300 is important for activity and stability of branching enzyme from Escherichia coli.PMID 11368019Read ↗

Alanine 310 is important for the activity of 1,4-α-glucan branching enzyme from Geobacillus thermoglucosidans STB02.Semantic proximity Read ↗

Function of second glucan binding site including tyrosines 54 and 101 in Thermus aquaticus amylomaltase.Semantic proximity Read ↗

Met349 Mutations Enhance the Activity of 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02.Semantic proximity Read ↗

Engineering of Thermal Stability in a Cold-Active Oligo-1,6-Glucosidase from Exiguobacterium sibiricum with Unusual Amino Acid Content.Semantic proximity Read ↗

A thermophilic alkalophilic α-amylase from Bacillus sp. AAH-31 shows a novel domain organization among glycoside hydrolase family 13 enzymes.Semantic proximity Read ↗

Alpha-amylase from Bacillus licheniformis mutants near to the catalytic site: effects on hydrolytic and transglycosylation activity.Semantic proximity Read ↗

Structural elements to convert Escherichia coli alpha-xylosidase (YicI) into alpha-glucosidase.Semantic proximity Read ↗

A multifunctional α-amylase BSGH13 from Bacillus subtilis BS-5 possessing endoglucanase and xylanase activities.Semantic proximity Read ↗

Effect of mutations to amino acid A301 and F361 in thermostability and catalytic activity of the β-galactosidase from Bacillus subtilis VTCC-DVN-12-01.Semantic proximity Read ↗

Improvement of enzymatic properties of Rhizopus oryzae α-amylase by site-saturation mutagenesis of histidine 286.Semantic proximity Read ↗

The fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activity.Semantic proximity Read ↗

Significance of H461 at subsite +1 in substrate binding and transglucosylation activity of amylomaltase from Corynebacterium glutamicum.Semantic proximity Read ↗

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