Molecular identification of carnosine N-methyltransferase as chicken histamine N-methyltransferase-like protein (hnmt-like).

Anserine (beta-alanyl-N(Pi)-methyl-L-histidine), a naturally occurring derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of skeletal muscles and brain of many vertebrates. Although it has long been proposed to serve as a proton buffer, radicals scavenger and transglycatin...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Jakub Drozak, Lukasz Chrobok, Olga Poleszak, Adam K Jagielski, Rafal Derlacz
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/638a68d87a1f49d1ab996341015ab914
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:638a68d87a1f49d1ab996341015ab914
record_format	dspace
spelling	oai:doaj.org-article:638a68d87a1f49d1ab996341015ab9142021-11-18T07:45:03ZMolecular identification of carnosine N-methyltransferase as chicken histamine N-methyltransferase-like protein (hnmt-like).1932-620310.1371/journal.pone.0064805https://doaj.org/article/638a68d87a1f49d1ab996341015ab9142013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23705015/?tool=EBIhttps://doaj.org/toc/1932-6203Anserine (beta-alanyl-N(Pi)-methyl-L-histidine), a naturally occurring derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of skeletal muscles and brain of many vertebrates. Although it has long been proposed to serve as a proton buffer, radicals scavenger and transglycating agent, its physiological function remains obscure. The formation of anserine is catalyzed by carnosine N-methyltransferase which exhibits unknown molecular identity. In the present investigation, we have purified carnosine N-methyltransferase from chicken pectoral muscle about 640-fold until three major polypeptides of about 23, 26 and 37 kDa coeluting with the enzyme were identified in the preparation. Mass spectrometry analysis of these polypeptides resulted in an identification of histamine N-methyltransferase-like (HNMT-like) protein as the only meaningful candidate. Analysis of GenBank database records indicated that the hnmt-like gene might be a paralogue of histamine N-methyltransferase gene, while comparison of their protein sequences suggested that HNMT-like protein might have acquired a new activity. Chicken HNMT-like protein was expressed in COS-7 cells, purified to homogeneity, and shown to catalyze the formation of anserine as confirmed by both chromatographic and mass spectrometry analysis. Both specificity and kinetic studies carried out on the native and recombinant enzyme were in agreement with published data. Particularly, several compounds structurally related to carnosine, including histamine and L-histidine, were tested as potential substrates for the enzyme, and carnosine was the only methyl group acceptor. The identification of the gene encoding carnosine N-methyltransferase might be beneficial for estimation of the biological functions of anserine.Jakub DrozakLukasz ChrobokOlga PoleszakAdam K JagielskiRafal DerlaczPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 5, p e64805 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jakub Drozak Lukasz Chrobok Olga Poleszak Adam K Jagielski Rafal Derlacz Molecular identification of carnosine N-methyltransferase as chicken histamine N-methyltransferase-like protein (hnmt-like).
description	Anserine (beta-alanyl-N(Pi)-methyl-L-histidine), a naturally occurring derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of skeletal muscles and brain of many vertebrates. Although it has long been proposed to serve as a proton buffer, radicals scavenger and transglycating agent, its physiological function remains obscure. The formation of anserine is catalyzed by carnosine N-methyltransferase which exhibits unknown molecular identity. In the present investigation, we have purified carnosine N-methyltransferase from chicken pectoral muscle about 640-fold until three major polypeptides of about 23, 26 and 37 kDa coeluting with the enzyme were identified in the preparation. Mass spectrometry analysis of these polypeptides resulted in an identification of histamine N-methyltransferase-like (HNMT-like) protein as the only meaningful candidate. Analysis of GenBank database records indicated that the hnmt-like gene might be a paralogue of histamine N-methyltransferase gene, while comparison of their protein sequences suggested that HNMT-like protein might have acquired a new activity. Chicken HNMT-like protein was expressed in COS-7 cells, purified to homogeneity, and shown to catalyze the formation of anserine as confirmed by both chromatographic and mass spectrometry analysis. Both specificity and kinetic studies carried out on the native and recombinant enzyme were in agreement with published data. Particularly, several compounds structurally related to carnosine, including histamine and L-histidine, were tested as potential substrates for the enzyme, and carnosine was the only methyl group acceptor. The identification of the gene encoding carnosine N-methyltransferase might be beneficial for estimation of the biological functions of anserine.
format	article
author	Jakub Drozak Lukasz Chrobok Olga Poleszak Adam K Jagielski Rafal Derlacz
author_facet	Jakub Drozak Lukasz Chrobok Olga Poleszak Adam K Jagielski Rafal Derlacz
author_sort	Jakub Drozak
title	Molecular identification of carnosine N-methyltransferase as chicken histamine N-methyltransferase-like protein (hnmt-like).
title_short	Molecular identification of carnosine N-methyltransferase as chicken histamine N-methyltransferase-like protein (hnmt-like).
title_full	Molecular identification of carnosine N-methyltransferase as chicken histamine N-methyltransferase-like protein (hnmt-like).
title_fullStr	Molecular identification of carnosine N-methyltransferase as chicken histamine N-methyltransferase-like protein (hnmt-like).
title_full_unstemmed	Molecular identification of carnosine N-methyltransferase as chicken histamine N-methyltransferase-like protein (hnmt-like).
title_sort	molecular identification of carnosine n-methyltransferase as chicken histamine n-methyltransferase-like protein (hnmt-like).
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/638a68d87a1f49d1ab996341015ab914
work_keys_str_mv	AT jakubdrozak molecularidentificationofcarnosinenmethyltransferaseaschickenhistaminenmethyltransferaselikeproteinhnmtlike AT lukaszchrobok molecularidentificationofcarnosinenmethyltransferaseaschickenhistaminenmethyltransferaselikeproteinhnmtlike AT olgapoleszak molecularidentificationofcarnosinenmethyltransferaseaschickenhistaminenmethyltransferaselikeproteinhnmtlike AT adamkjagielski molecularidentificationofcarnosinenmethyltransferaseaschickenhistaminenmethyltransferaselikeproteinhnmtlike AT rafalderlacz molecularidentificationofcarnosinenmethyltransferaseaschickenhistaminenmethyltransferaselikeproteinhnmtlike
_version_	1718423040128188416

Molecular identification of carnosine N-methyltransferase as chicken histamine N-methyltransferase-like protein (hnmt-like).

Ejemplares similares