CARNMT1

Last update 08 May 2025

Basic Info

Synonyms

C9orf41, CARNMT1, Carnosine N-methyltransferase

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Introduction

N-methyltransferase that catalyzes the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).

100 Clinical Results associated with CARNMT1

100 Translational Medicine associated with CARNMT1

0 Patents (Medical) associated with CARNMT1

Literatures (Medical) associated with CARNMT1

01 Oct 2023·Physiological Reports

Anserine is expressed in human cardiac and skeletal muscles

Article

Author: Vargas, Bianca Scigliano ; Carvalho, Victor Henrique ; Pereira, Wagner Ribeiro ; de Medeiros, Marisa Helena Gennari ; da Silva, Rafael Pires ; Roschel, Hamilton ; de Souza Gonçalves, Lívia ; Yamaguchi, Guilherme Carvalho ; Artioli, Guilherme Giannini ; Jensen, Leonardo

AbstractWe evaluated whether anserine, a methylated analog of the dipeptide carnosine, is present in the cardiac and skeletal muscles of humans and whether the CARNMT1 gene, which encodes the anserine synthesizing enzyme carnosine‐N‐methyltransferase, is expressed in human skeletal muscle. We found that anserine is present at low concentrations (low micromolar range) in both cardiac and skeletal muscles, and that anserine content in skeletal muscle is ~15 times higher than in cardiac muscle (cardiac muscle: 10.1 ± 13.4 μmol·kg−1 of dry muscle, n = 12; skeletal muscle: 158.1 ± 68.5 μmol·kg−1 of dry muscle, n = 11, p < 0.0001). Anserine content in the heart was highly variable between individuals, ranging from 1.4 to 45.4 μmol·kg−1 of dry muscle, but anserine content was not associated with sex, age, or body mass. We also showed that CARNMT1 gene is poorly expressed in skeletal muscle (n = 10). This is the first study to demonstrate that anserine is present in the ventricle of the human heart. The presence of anserine in human heart and the confirmation of its expression in human skeletal muscle open new avenues of investigation on the specific and differential physiological functions of histidine dipeptides in striated muscles.

01 Aug 2023·Genes & development

Histidine N1-position-specific methyltransferase CARNMT1 targets C3H zinc finger proteins and modulates RNA metabolism.

Article

Author: Kotoshiba, Kaoru ; Sohtome, Yoshihiro ; Suzuki, Takehiro ; Akakabe, Mai ; Sodeoka, Mikiko ; Yoshimoto, Rei ; Dohmae, Naoshi ; Shimazu, Tadahiro ; Matoba, Shogo ; Shinkai, Yoichi ; Hirose, Michiko ; Ogura, Atsuo

Histidine (His) residues are methylated in various proteins, but their roles and regulation mechanisms remain unknown. Here, we show that carnosine N-methyltransferase 1 (CARNMT1), a known His methyltransferase of dipeptide carnosine (βAla-His), is a major His N1-position-specific methyltransferase. We found that 52 His sites in 20 proteins underwent CARNMT1-mediated methylation. The consensus methylation site for CARNMT1 was identified as Cx(F/Y)xH, a C3H zinc finger (C3H ZF) motif. CARNMT1-deficient and catalytically inactive mutant mice showed embryonic lethality. Among the CARNMT1 target C3H ZF proteins, RNA degradation mediated by Roquin and tristetraprolin (TTP) was affected by CARNMT1 and its enzymatic activity. Furthermore, the recognition of the 3' splice site of the CARNMT1 target C3H ZF protein U2AF1 was perturbed, and pre-mRNA alternative splicing (AS) was affected by CARNMT1 deficiency. These findings indicate that CARNMT1-mediated protein His methylation, which is essential for embryogenesis, plays roles in diverse aspects of RNA metabolism by targeting C3H ZF-type RNA-binding proteins and modulating their functions, including pre-mRNA AS and mRNA degradation regulation.

01 Aug 2023·Genes & Development

Putting a finger on histidine methylation

Article

Author: Boutz, Paul L

Specialized enzymes add methyl groups to the nitrogens of the amino acid histidine, altering the chemical properties of its imidazole ring and, in turn, the function of the modified (poly)peptide. In this issue ofGenes & Development, Shimazu and colleagues (pp. 724–742) make the remarkable discovery that CARNMT1 acts as a dual-specificity histidine methyltransferase, modifying both the small-molecule dipeptide carnosine and a set of proteins, predominantly within RNA-binding C3H zinc finger (C3H ZF) motifs. As a result, CARNMT1 modulates the activity of its protein targets to affect RNA processing and metabolism, ultimately contributing an essential function during mammalian development.

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CARNMT1

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