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

Active site lysine promotes catalytic function of pyridoxal 5'-phosphate in alpha-glucan phosphorylases.

The Journal of biological chemistry - 25 May 1991

Schinzel R

Abstract excerpt

Tight contact of pyridoxal 5'-phosphate to the substrate phosphate is considered to be a crucial requirement of the phosphorolytic cleavage of polysaccharides by glycogen phosphorylases. This study demonstrates an essential role of lysine 533, the only charged residue in hydrogen bond distance to...

Topics

Amino Acid Sequence
Binding Sites
Catalysis
Cations
Escherichia coli
Glucosyltransferases
Kinetics
Lysine
Molecular Sequence Data
Mutation
Phosphorylases
Pyridoxal Phosphate

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 1827794

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1827794-2026-08-30.1. 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.

0

discussions

0

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

Active site lysine promotes catalytic function of pyridoxal 5'-phosphate in alpha-glucan phosphorylases.PMID 1827794Read ↗

Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies.Semantic proximity Read ↗

Factors affecting oligomerization status of UDP-glucose pyrophosphorylase.Semantic proximity Read ↗

Barley alpha-amylase Met53 situated at the high-affinity subsite -2 belongs to a substrate binding motif in the beta-->alpha loop 2 of the catalytic (beta/alpha)8-barrel and is critical for activity and substrate specificity.Semantic proximity Read ↗

Conserved arginine-516 of Penicillium amagasakiense glucose oxidase is essential for the efficient binding of beta-D-glucose.Semantic proximity Read ↗

Mutations in the active site of Escherichia coli phosphofructokinase.Semantic proximity Read ↗

Functions of the conserved anionic amino acids and those interacting with the substrate phosphate group of phosphoglucose isomerase.Semantic proximity Read ↗

Catalytic site of F1-ATPase of Escherichia coli. Lys-155 and Lys-201 of the beta subunit are located near the gamma-phosphate group of ATP in the presence of Mg2+.Semantic proximity Read ↗

The phosphate site of trehalose phosphorylase from Schizophyllum commune probed by site-directed mutagenesis and chemical rescue studies.Semantic proximity Read ↗

Asp48 function in the hydrogen-bonding network involving Asp52 of hen egg-white lysozyme.Semantic proximity Read ↗

Identification of a catalytic residue of Clostridium paraputrificum N-acetyl-beta-D-glucosaminidase Nag3A by site-directed mutagenesis.Semantic proximity Read ↗

Role of Phe283 in enzymatic reaction of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp.1011: Substrate binding and arrangement of the catalytic site.Semantic proximity Read ↗

Asp-196-->Ala mutant of Leuconostoc mesenteroides sucrose phosphorylase exhibits altered stereochemical course and kinetic mechanism of glucosyl transfer to and from phosphate.Semantic proximity Read ↗

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