![conference banner](/images/conference-banner.jpeg)
Abstract
A previously uncharacterized member of the M1 family of zinc metallopeptidases, arginyl aminopeptidase-like 1 (RNPEPL1; EC 3.4.11.1), was cloned and expressed, and the recombinant enzyme characterized. RNPEPL1 was a broad specificity aminopeptidase with preference for a P1 methionine, glutamine, or citrulline residue, and exhibited a broad pH preference, with maximal activity observed between pH 6.6 and 8.0. The enzyme was inhibited by calcium ions but unaffected by chloride ions, and was insensitive to specific inhibitors of the closely-related arginyl aminopeptidase, indicating similarity to leukotriene A4 hydrolase. RT-PCR analysis of RNPEPL1 expression revealed a ubiquitous tissue distribution, consistent with a general housekeeping function, but also revealed alternative splicing of the mRNA in all tissues examined. The inclusion of intron 5 was predicted to result in a truncated protein product, while an alternative 3 ’ splice site of exon 9 of the reference sequence was predicted to result in the omission of a conserved eleven amino acid stretch from the C-terminal domain.
Keywords: alternative splicing, calcium, zinc, protease, metallopeptidase, Aminopeptidase
Protein & Peptide Letters
Title: Arginyl Aminopeptidase-Like 1 (RNPEPL1) Is an Alternatively Processed Aminopeptidase with Specificity for Methionine, Glutamine, and Citrulline Residues
Volume: 16 Issue: 10
Author(s): Michael W. Thompson, Karen A. Beasley, Matthew D. Schmidt and Rebecca L. Seipelt
Affiliation:
Keywords: alternative splicing, calcium, zinc, protease, metallopeptidase, Aminopeptidase
Abstract: A previously uncharacterized member of the M1 family of zinc metallopeptidases, arginyl aminopeptidase-like 1 (RNPEPL1; EC 3.4.11.1), was cloned and expressed, and the recombinant enzyme characterized. RNPEPL1 was a broad specificity aminopeptidase with preference for a P1 methionine, glutamine, or citrulline residue, and exhibited a broad pH preference, with maximal activity observed between pH 6.6 and 8.0. The enzyme was inhibited by calcium ions but unaffected by chloride ions, and was insensitive to specific inhibitors of the closely-related arginyl aminopeptidase, indicating similarity to leukotriene A4 hydrolase. RT-PCR analysis of RNPEPL1 expression revealed a ubiquitous tissue distribution, consistent with a general housekeeping function, but also revealed alternative splicing of the mRNA in all tissues examined. The inclusion of intron 5 was predicted to result in a truncated protein product, while an alternative 3 ’ splice site of exon 9 of the reference sequence was predicted to result in the omission of a conserved eleven amino acid stretch from the C-terminal domain.
Export Options
About this article
Cite this article as:
Thompson Michael W., Beasley Karen A., Schmidt Matthew D. and Seipelt Rebecca L., Arginyl Aminopeptidase-Like 1 (RNPEPL1) Is an Alternatively Processed Aminopeptidase with Specificity for Methionine, Glutamine, and Citrulline Residues, Protein & Peptide Letters 2009; 16 (10) . https://dx.doi.org/10.2174/092986609789071199
DOI https://dx.doi.org/10.2174/092986609789071199 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
![Wayfinder Image](/images/wayfinder.jpg)
- Author Guidelines
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers
Related Articles
-
Intracellular Bioinorganic Chemistry and Cross Talk Among Different -Omics
Current Topics in Medicinal Chemistry Practical Aspects in the Use of Biomarkers for the Development of Cancer Vaccines
Current Cancer Therapy Reviews Superior Anticancer Potential of Nano-Paclitaxel Combined Bevacizumab Treatment in Ovarian Cancer
Current Pharmaceutical Biotechnology Merging Transport Data for Choroid Plexus with Blood-Brain Barrier to Model CNS Homeostasis and Disease More Effectively
CNS & Neurological Disorders - Drug Targets The Acetyltransferase KAT5 Inhibitor NU 9056 Promotes Apoptosis and Inhibits JAK2/STAT3 Pathway in Extranodal NK/T Cell Lymphoma
Anti-Cancer Agents in Medicinal Chemistry Progress in the Development of Selective Inhibitors of Aurora Kinases
Current Topics in Medicinal Chemistry PET and SPECT Radiotracers to Assess Function and Expression of ABC Transporters In Vivo
Current Drug Metabolism Will Arsenic Trioxide Benefit Treatment of Solid Tumor by Nano- Encapsulation?
Mini-Reviews in Medicinal Chemistry Gene Therapy Using IL-12 Family Members in Infection, Auto-Immunity, and Cancer
Current Gene Therapy Cancer Gene Therapy through Autonomous Parvovirus - Mediated Gene Transfer
Current Gene Therapy Recombinant Adeno-associated Virus 9-mediated Expression of Kallistatin Suppresses Lung Tumor Growth in Mice
Current Gene Therapy Virus-Like Particles as Particulate Vaccines
Current HIV Research Epoxycarotenoids and Cancer. Review
Current Bioactive Compounds Anticancer Agents Derived from Natural Products
Mini-Reviews in Medicinal Chemistry Patent Selections
Recent Patents on Biomarkers Breast Cancer Diagnosis Using Data Mining Methods, Cumulative Histogram Features, and Gary Level Co-occurrence Matrix
Current Medical Imaging Artepillin C Induces Selective Oxidative Stress and Inhibits Migration and Invasion in a Comprehensive Panel of Human Cervical Cancer Cell Lines
Anti-Cancer Agents in Medicinal Chemistry Novel Mechanisms of Anticancer Activities of Green Tea Component Epigallocatechin- 3-Gallate
Anti-Cancer Agents in Medicinal Chemistry Synthesis and In Vitro Anticancer Activity of Novel 2-((3-thioureido)carbonyl) phenyl Acetate Derivatives
Letters in Drug Design & Discovery Advancements in Treatment Options of Women Infertility
Current Women`s Health Reviews