ArticleThe Journal of biological chemistry2009
Histidine 379 of human laeverin/aminopeptidase Q, a nonconserved residue within the exopeptidase motif, defines its distinctive enzymatic properties.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Laeverin is Cell-Surface Target for Liquid-Phase Metastasizing Cancer Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Amniotic Fluid and Maternal Serum Laeverin Levels and Their Correlations with Fetal Size and Placental Volume in Second Trimester of Pregnancy-A Prospective Cross-Sectional Study.Diagnostics (Basel, Switzerland) · 2025Article
- Article
- PRG2 and AQPEP are misexpressed in fetal membranes in placenta previa and percreta†.Biology of reproduction · 2021Article
- Importance of Tyr409 and Tyr414 in constructing the substrate pocket of human aminopeptidase B.Molecular and cellular biochemistry · 2020Article
- Promoting Roles of Embryonic Signals in Embryo Implantation and Placentation in Cooperation with Endocrine and Immune Systems.International journal of molecular sciences · 2020Review
- Lvrn expression is not critical for mouse placentation.The Journal of reproduction and development · 2019Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human laeverin/aminopeptidase Q (LVRN/APQ) is a novel member of the M1 family of zinc aminopeptidases and is specifically expressed on the cell surface of human extravillous trophoblasts. Multiple sequence alignment of human M1 aminopeptidase revealed that the first Gly residue within the conserved exopeptidase motif of the M1 family, GXMEN motif, is uniquely substituted for His in human LVRN/APQ. In this study, we evaluated the roles of nonconserved His(379), comprising the exopeptidase motif in the enzymatic properties of human LVRN/APQ. We revealed that the substitution of His(379) with Gly caused significant changes in substrate specificity both toward fluorogenic substrates and natural peptide hormones. In addition, the susceptibilities of bestatin, a sensitive inhibitor for human LVRN/APQ, and natural inhibitory peptides were decreased in the H379G mutant. A molecular model suggested a conformational difference between wild-type and H379G human LVRN/APQs. These results indicate that His(379) of the enzyme plays essential roles in its distinctive enzymatic properties and contributes to maintaining the appropriate structure of the catalytic cavity of the enzyme. Our data may bring new insight into the biological significance of the unique exopeptidase motif of LVRN/APQ obtained during the evolution of primates.
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