3-Amino-2-hydroxy-propionaldehyde and 3-amino-1-hydroxy-propan-2-one derivatives: new classes of aminopeptidase inhibitors.

doi:10.1016/0968-0896(96)00115-0

Paper

DOI: 10.1016/0968-0896(96)00115-0

3-Amino-2-hydroxy-propionaldehyde and 3-amino-1-hydroxy-propan-2-one derivatives: new classes of aminopeptidase inhibitors.

Published Aug 1, 1996 · C. Tarnus, J. M. Remy, H. D'orchymont

Bioorganic & medicinal chemistry

Q2 SJR score

Citations

Influential Citations

Full textSemantic Scholar

Abstract

Abstract hidden due to publisher request; this does not indicate any issues with the research. Click the full text link above to read the abstract and view the original source.

Study Snapshot

3-amino-2-hydroxy-propionaldehydes and 3-amino-1-hydroxy-propan-2-one derivatives show potential as new classes of aminopeptidase inhibitors, with potential for use in pharmaceutical and biotechnology applications.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

Sign up to use Study Snapshot

Consensus is limited without an account. Create an account or sign in to get more searches and use the Study Snapshot.

Create an account

Full text analysis coming soon...

References

DOI: 10.1006/ABBI.1994.1206

3-Amino-2-tetralone derivatives: novel potent and selective inhibitors of aminopeptidase-M (EC 3.4.11.2).

3-amino-2-tetralone derivatives are potent and selective inhibitors of aminopeptidase-M, aiding in identifying new endogenous substrates and clarifying its physiological or pathophysiological role.

1994·36citations·C. Schalk et al.·Archives of biochemistry and biophysics

Archives of biochemistry and biophysics

DOI: 10.1016/S0969-2126(00)00030-7

Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family.

The crystal structure of Aeromonas proteolytica aminopeptidase suggests that two zinc ions form a co-catalytic unit and play equivalent roles during catalysis, contradicting previous findings.

1994·211citations·B. Chevrier et al.·Structure

Structure

DOI: 10.1016/0003-9861(92)90141-I

Rapid purification of the Aeromonas proteolytica aminopeptidase: crystallization and preliminary X-ray data.

Aeromonas proteolytica aminopeptidase can be rapidly purified using two new procedures, resulting in large crystals for X-ray analysis.

1992·22citations·C. Schalk et al.·Archives of biochemistry and biophysics

Archives of biochemistry and biophysics

DOI: 10.1016/0006-2952(90)90348-O

Metabolism of vasoactive peptides by plasma and purified renal aminopeptidase M.

Aminopeptidase M plays a significant role in the metabolism of circulating vasoactive peptides, with optimal degradation at neutral pH and inhibition by amastatin and bestatin.

1990·102citations·P. Ward et al.·Biochemical pharmacology

Biochemical pharmacology

DOI: 10.1016/s0026-895x(25)10218-6

Characterization of aminopeptidases responsible for inactivating endogenous (Met5)enkephalin in brain slices using peptidase inhibitors and anti-aminopeptidase M antibodies.

Aminopeptidase M plays a largely predominant role in endogenous (Met5)enkephalin degradation in brain slices, while both "enkephalinase" and "puromycin-sensitive" aminopeptidases participate in the process.

1986·97citations·B. Giros et al.·Molecular pharmacology

Molecular pharmacology

DOI: 10.1016/s0021-9258(17)38851-8

The slow, tight binding of bestatin and amastatin to aminopeptidases.

Bestatin and amastatin exhibit slow, tight binding to various aminopeptidases, suggesting the formation of a transition state analog complex between enzyme and inhibitor.

1985·83citations·S. Wilkes et al.·The Journal of biological chemistry

The Journal of biological chemistry

DOI: 10.1021/BI00323A014

Use of secondary isotope effects and varying pH to investigate the mode of binding of inhibitory amino aldehydes by leucine aminopeptidase.

Leucine aldehyde binds to leucine aminopeptidase as an oxygen adduct, not as the intact aldehyde, suggesting it acts as an inhibitor rather than a substrate.

1985·16citations·Lars Andersson et al.·Biochemistry

Biochemistry

DOI: 10.1016/s0021-9258(17)43944-5

Stereospecificity of amino acid hydroxamate inhibition of aminopeptidases.

D isomers of amino acid hydroxamates effectively inhibit cytosolic leucine aminopeptidase and Aeromonas enzyme, with manganese-activated kidney cytosolic leucine aminopeptidase being more effectively inhibited by D isomers than L isomers.

1983·30citations·S. Wilkes et al.·The Journal of biological chemistry

The Journal of biological chemistry

Citations

DOI: 10.1371/journal.pone.0050639

Functional Characterization of Two M42 Aminopeptidases Erroneously Annotated as Cellulases

M42 aminopeptidases, including CelM and TmPep1050, are not cellulases, and their homology with CelM suggests they may play a role in proteasome degradation.

2012·13citations·R. Dutoit et al.·PLoS ONE

PLoS ONE

DOI: 10.1016/j.biochi.2010.04.026

Metallo-aminopeptidase inhibitors

This paper presents various approaches for designing inhibitors for metallo-aminopeptidases, which could lead to potential drug discovery against endogenous and infectious diseases.

2010·123citations·A. Mucha et al.·Biochimie

Biochimie

DOI: 10.1002/JCCS.200800134

A Convenient and Versatile Method for the Preparation of α-Hydroxymethyl Ketone Derivatives from the Corresponding Allyl Silyl Ethers or Allyl Carboxylates

This study presents a convenient and versatile method for preparing -hydroxymethyl ketones from 1-substituted allyl silyl ethers or allyl carboxylates, yielding -silyloxymethyl- or a-acyloxymethyl-ketones in good yield

2008·6citations·Y. Hon et al.·Journal of The Chinese Chemical Society

Journal of The Chinese Chemical Society

DOI: 10.1002/med.20044

Aminopeptidase‐N/CD13 (EC 3.4.11.2) inhibitors: Chemistry, biological evaluations, and therapeutic prospects

Inhibiting APN/CD13 may lead to the development of anti-cancer and anti-inflammatory drugs, with potential toxicity and specificity discussed.

2005·238citations·B. Bauvois et al.·Medicinal Research Reviews

Medicinal Research Reviews

DOI: 10.1016/J.TET.2004.06.060

Stereoselective synthesis of constrained oxacyclic hydroxyethylene isosteres of aspartyl protease inhibitors. Nitroaldol methodology toward 2,3-substituted tetrahydrofurans

This study successfully synthesized constrained oxacyclic hydroxyethylene isosteres of aspartyl protease inhibitors using Binol lanthanide and Trost dinuclear zinc catalysts, providing insights into their structure and function.

2004·12citations·S. Hanessian et al.·Tetrahedron

Tetrahedron

DOI: 10.1139/V04-010

3-Amino-1-hydroxyacetone

This study successfully prepared 3-amino-1-hydroxyacetone (52% yield) in 6 steps using N-phthaloylglycine, making it adaptable for bond-labeled samples.

2004·3citations·N. Ullah et al.·Canadian Journal of Chemistry

Canadian Journal of Chemistry

DOI: 10.3109/14756369909030321

Novel small molecule nonpeptide aminopeptidase n inhibitors with a cyclic imide skeleton.

N-phenylhomophthalimide analogs are specific and potent inhibitors of aminopeptidase N, with PIQ-22 showing potent tumor-cell invasion inhibitory activity.

1999·33citations·R. Shimazawa et al.·Journal of enzyme inhibition

Journal of enzyme inhibition