(Q27679264)

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A Naturally Variable Residue in the S1 Subsite of M1 Family Aminopeptidases Modulates Catalytic Properties and Promotes Functional Specialization

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scholarly article

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A Naturally Variable Residue in the S1 Subsite of M1 Family Aminopeptidases Modulates Catalytic Properties and Promotes Functional Specialization (English)

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M1-family alanyl aminopeptidase

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11 September 2018

author name string

Seema Dalal

1

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Daniel R T Ragheb

2

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Florian D Schubot

3

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Michael Klemba

4

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language of work or name

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publication date

6 September 2013

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Journal of Biological Chemistry

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288

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36

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26004-12

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The crystal structure of human endoplasmic reticulum aminopeptidase 2 reveals the atomic basis for distinct roles in antigen processing

1 reference

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Bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases

1 reference

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20 March 2017

Structure of aminopeptidase N from Escherichia coli complexed with the transition-state analogue aminophosphinic inhibitor PL250

1 reference

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20 March 2017

Structural basis for the inhibition of the essential Plasmodium falciparum M1 neutral aminopeptidase

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Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design

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Structural basis for the unusual specificity of Escherichia coli aminopeptidase N

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20 March 2017

Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases

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20 March 2017

Genome sequence of the human malaria parasite Plasmodium falciparum

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Automated structure solution with the PHENIX suite

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WebLogo: A Sequence Logo Generator

1 reference

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LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3764805

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On the size of the active site in proteases. I. Papain

1 reference

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Distribution and biochemical properties of an M1-family aminopeptidase in Plasmodium falciparum indicate a role in vacuolar hemoglobin catabolism

1 reference

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Roles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparum

1 reference

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A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation

1 reference

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An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides

1 reference

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ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3764805

20 March 2017

Engagement of the S1, S1' and S2' subsites drives efficient catalysis of peptide bond hydrolysis by the M1-family aminopeptidase from Plasmodium falciparum

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3764805

29 September 2017

Probing the S1 specificity pocket of the aminopeptidases that generate antigenic peptides.

1 reference

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29 September 2017

Endoplasmic reticulum aminopeptidases: Biology and pathogenic potential

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3764805

29 September 2017

Aminopeptidase fingerprints, an integrated approach for identification of good substrates and optimal inhibitors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3764805

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A new role for Zn(II) aminopeptidases: antigenic peptide generation and destruction.

1 reference

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Arginyl aminopeptidase-like 1 (RNPEPL1) is an alternatively processed aminopeptidase with specificity for methionine, glutamine, and citrulline residues

1 reference

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Evolution of peptidase diversity

1 reference

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The moonlighting enzyme CD13: old and new functions to target

1 reference

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Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site

1 reference

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The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a "molecular ruler" mechanism.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3764805

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Plasmodium falciparum PfA-M1 aminopeptidase is trafficked via the parasitophorous vacuole and marginally delivered to the food vacuole

1 reference

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2 June 2018

Novel selective inhibitors of the zinc plasmodial aminopeptidase PfA-M1 as potential antimalarial agents.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M113.465625

21 January 2018

Catalytic activity of Peptidase N is required for adaptation of Escherichia coli to nutritional downshift and high temperature stress.

1 reference

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Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition.

1 reference

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NMRPipe: a multidimensional spectral processing system based on UNIX pipes

1 reference

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PROCHECK: a program to check the stereochemical quality of protein structures

1 reference

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Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum.

1 reference

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Processing of X-ray diffraction data collected in oscillation mode

1 reference

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1 reference

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