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

Substrate recognition mechanism of prolyl aminopeptidase from Serratia marcescens.

Journal of biochemistry - 1 Oct 2000

Ito K, Inoue T, Kabashima T, Kanada N, Huang H S, Ma X, Azmi N, Azab E, Yoshimoto T

Abstract excerpt

Molecular cloning of the gene and the crystal structure of the prolyl aminopeptidase [EC 3.4.11.5] from Serratia marcescens have been studied by us [J. Biochem. 122, 601-605 (1997); ibid. 126, 559-565 (1999)]. Through these studies, Phe139, Tyr149, Glu204, and Arg136 were estimated to be concerned with substrate recognition. To elucidate the details of the mechanism for the substrate specificity, the...

Read the complete abstract on PubMed

Topics

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

Share to Aminopeptidases
Share to Catalysis
Share to Cysteine

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

Share to Peptides

Share to Proline

Share to Protein Structure, Secondary

Share to Serratia marcescens

Share to Substrate Specificity

Source

Identifiers

PMID: 11011150
DOI: 10.1093/oxfordjournals.jbchem.a022800

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

Substrate recognition mechanism of prolyl aminopeptidase from Serratia marcescens.PMID 11011150Read ↗

Activity modulation of the oligopeptidase B from Serratia proteamaculans by site-directed mutagenesis of amino acid residues surrounding catalytic triad histidine.Semantic proximity Read ↗

Novel inhibitor for prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis and details of substrate-recognition mechanism.Semantic proximity Read ↗

Effects of Distal Mutations on Prolyl-Adenylate Formation of Escherichia coli Prolyl-tRNA Synthetase.Semantic proximity Read ↗

The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli.Semantic proximity Read ↗

Mutation of active site serine residue with cysteine displays change in acyl-acceptor preference of β-peptidyl aminopeptidase from Pseudomonas aeruginosa PAO1.Semantic proximity Read ↗

Involvement of the COOH-terminal pro-sequence of Serratia marcescens serine protease in the folding of the mature enzyme.Semantic proximity Read ↗

Characterization and rational design for substrate specificity of a prolyl endopeptidase from Stenotrophomonas maltophilia.Semantic proximity Read ↗

Studies on the molecular docking and amino Acid residues involving in recognition of substrate in proline iminopeptidase by site-directed mutagenesis.Semantic proximity Read ↗

Mutation of H63 and its catalytic affect on the methionine aminopeptidase from Escherichia coli.Semantic proximity Read ↗

Roles of asp126 and asp156 in the enzyme function of sphingomyelinase from Bacillus cereus.Semantic proximity Read ↗

Change in substrate preference of Streptomyces aminopeptidase through modification of the environment around the substrate binding site.Semantic proximity Read ↗

The metalloprotease gene of Serratia marcescens strain SM6.Semantic proximity Read ↗

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