Discover Community Create You

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

Substitutions of glycine residues Gly100 and Gly147 in conservative loops decrease rates of conformational rearrangements of Escherichia coli inorganic pyrophosphatase.

Biochemistry. Biokhimiia - 1 Aug 2005

Moiseev V M, Rodina E V, Kurilova S A, Vorobyeva N N, Nazarova T I, Avaeva S M

Abstract excerpt

Escherichia coli inorganic pyrophosphatase (PPase) is a one-domain globular enzyme characterized by its ability to easily undergo minor structure rearrangements involving flexible segments of the polypeptide chain. To elucidate a possible role of these segments in catalysis, catalytic properties of mutant variants of E. coli PPase Gly100Ala and Gly147Val with substitutions in the conservative loops II and III...

Read the complete abstract on PubMed

Topics

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

Share to Binding, Competitive
Share to Catalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Conserved Sequence

Share to Diphosphates

Share to Glycine

Share to Hydrogen-Ion Concentration

Share to Hydrolysis

Share to Magnesium

Source

Identifiers

PMID: 16212541
DOI: 10.1007/s10541-005-0195-z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Substitutions of glycine residues Gly100 and Gly147 in conservative loops decrease rates of conformational rearrangements of Escherichia coli inorganic pyrophosphatase.PMID 16212541Read ↗

Effect of mutation of the conservative glycine residues Gly100 and Gly147 on stability of Escherichia coli inorganic pyrophosphatase.Semantic proximity Read ↗

Effect of Structure Variations in the Inter-subunit Contact Zone on the Activity and Allosteric Regulation of Inorganic Pyrophosphatase from Mycobacterium tuberculosis.Semantic proximity Read ↗

A site-directed mutagenesis study on Escherichia coli inorganic pyrophosphatase. Glutamic acid-98 and lysine-104 are important for structural integrity, whereas aspartic acids-97 and -102 are essential for catalytic activity.Semantic proximity Read ↗

On the functional role of Arg172 in substrate binding and allosteric transition in Escherichia coli glucosamine-6-phosphate deaminase.Semantic proximity Read ↗

Effectory site in Escherichia coli inorganic pyrophosphatase is revealed upon mutation at the intertrimeric interface.Semantic proximity Read ↗

ATP as effector of inorganic pyrophosphatase of Escherichia coli. The role of residue Lys112 in binding effectors.Semantic proximity Read ↗

Binding of substrate at the effector site of pyrophosphatase increases the rate of its hydrolysis at the active site.Semantic proximity Read ↗

Functional roles of arginine residues in mung bean vacuolar H+-pyrophosphatase.Semantic proximity Read ↗

Mutagenic analysis of functional residues in putative substrate-binding site and acidic domains of vacuolar H+-pyrophosphatase.Semantic proximity Read ↗

A complete structural description of the catalytic cycle of yeast pyrophosphatase.Semantic proximity Read ↗

Mutations in the hinge of a dynamic loop broadly influence functional properties of fructose-1,6-bisphosphatase.Semantic proximity Read ↗

Distance variations between active sites of H(+)-pyrophosphatase determined by fluorescence resonance energy transfer.Semantic proximity Read ↗

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