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

Mutational analysis of the reactive site loop of Streptomyces metalloproteinase inhibitor, SMPI.

Journal of biochemistry - 1 Jan 1999

Hiraga K, Seeram S S, Tate S, Tanaka N, Kainosho M, Oda K

Abstract excerpt

Streptomyces metalloproteinase inhibitor (SMPI) is the only inhibitor to show "standard mechanism inhibition" against metalloproteinases. SMPI is a globular protein with an exposed loop containing the reactive site, C64-V65. To analyze the importance of basic residues in the reactive site loop of SMPI, mutants were constructed for R60, K61, and R66 (R60A, K61A, R66A, R60/K61A, 60/61/66A, and 60/61/66E). The...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Binding Sites
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Magnetic Resonance Spectroscopy

Share to Models, Molecular

Share to Mutation

Share to Protein Conformation

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 9880818
DOI: 10.1093/oxfordjournals.jbchem.a022260

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutational analysis of the reactive site loop of Streptomyces metalloproteinase inhibitor, SMPI.PMID 9880818Read ↗

Effect of inhibitory activity of mutation at reaction site P4 of the Streptomyces subtilisin inhibitor, SSI.Semantic proximity Read ↗

Computational simulations assessment of mutations impact on streptokinase (SK) from a group G streptococci with enhanced activity - insights into the functional roles of structural dynamics flexibility of SK and stabilization of SK-μplasmin catalytic complex.Semantic proximity Read ↗

Preparation of a novel streptokinase mutant with improved stability.Semantic proximity Read ↗

Solution structure and backbone dynamics of streptopain: insight into diverse substrate specificity.Semantic proximity Read ↗

Binding characteristics of thrombin-activatable fibrinolysis inhibitor to streptococcal surface collagen-like proteins A and B.Semantic proximity Read ↗

Identification of the blood coagulation factor interacting sequences in staphylococcal superantigen-like protein 10.Semantic proximity Read ↗

Structures of importance for the stability of antiplasmin as studied by site-directed mutagenesis.Semantic proximity Read ↗

[Construction and activities of suilysin mutants].Semantic proximity Read ↗

Structure-function analysis of the streptokinase amino terminus (residues 1-59).Semantic proximity Read ↗

Alteration of the specificity of the Streptomyces subtilisin inhibitor by gene engineering.Semantic proximity Read ↗

A molecular model of the serine protease domain of activated protein C: application to the study of missense mutations causing protein C deficiency.Semantic proximity Read ↗

In silico mutations and molecular dynamics studies on a winged bean chymotrypsin inhibitor protein.Semantic proximity Read ↗

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