Limits...
Biochemical characterization of bovine brain myristoyl-CoA:protein N-myristoyltransferase type 2.

Selvakumar P, Lakshmikuttyamma A, Sharma RK - J. Biomed. Biotechnol. (2009)

Bottom Line: Kinetic studies suggested that bovine brain NMT2 and human NMT1 show significant differences in their peptide substrate specificities.The metal ion Ca(2+) had stimulatory effects on NMT2 activity while Mn(2+) and Zn(2+) inhibited the enzyme activity.In addition, NMT2 activity was inhibited by various organic solvents and other detergents while NMT1 had a stimulatory effect.

View Article: PubMed Central - PubMed

Affiliation: Department of Pathology and Laboratory Medicine, College of Medicine and Health Research Division, Saskatchewan Cancer Agency, University of Saskatchewan, SK, Canada.

ABSTRACT
Protein N-myristoylation is a lipidic modification which refers to the covalent attachment of myristate, a 14-carbon saturated fatty acid, to the N-terminal glycine residue of a number of mammalian, viral, and fungal proteins. In this paper, we have cloned the gene coding for myristoyl-CoA:protein N-myristoyltransferase (NMT) from Bos tarus brain. The open reading frame codes for a 410-amino-acid protein and overexpressed in Escherichia coli. Kinetic studies suggested that bovine brain NMT2 and human NMT1 show significant differences in their peptide substrate specificities. The metal ion Ca(2+) had stimulatory effects on NMT2 activity while Mn(2+) and Zn(2+) inhibited the enzyme activity. In addition, NMT2 activity was inhibited by various organic solvents and other detergents while NMT1 had a stimulatory effect. Biochemical characterization suggested that both forms of NMT have unique characteristics. Further analysis towards functional role NMT2 will lead the development of therapeutic target for the progression of various diseases such as cancer, cardiovascular diseases, and neurodegenerative diseases.

Show MeSH

Related in: MedlinePlus

Molecular phylogenetic tree of the amino acid sequences of NMT2s from various species. The tree was constructed by the neighbor joining method, based on sequence information.
© Copyright Policy - open-access
Related In: Results  -  Collection


getmorefigures.php?uid=PMC2737134&req=5

fig2: Molecular phylogenetic tree of the amino acid sequences of NMT2s from various species. The tree was constructed by the neighbor joining method, based on sequence information.

Mentions: Phylogenetic analysis of NMT2 family reveals that it can be grouped into three major families (Figure 2). Group one family is composed of proteins from A. thaliana, the second family consists of R. norvegicus, H. sapiens, and B. Taurus, and the third family consists of M. musculus. The second family further subgrouped into R. norvegicus, H. sapiens, and B. taurus. The phylogenetic tree suggested that B. taurus belongs to the second group.


Biochemical characterization of bovine brain myristoyl-CoA:protein N-myristoyltransferase type 2.

Selvakumar P, Lakshmikuttyamma A, Sharma RK - J. Biomed. Biotechnol. (2009)

Molecular phylogenetic tree of the amino acid sequences of NMT2s from various species. The tree was constructed by the neighbor joining method, based on sequence information.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2737134&req=5

fig2: Molecular phylogenetic tree of the amino acid sequences of NMT2s from various species. The tree was constructed by the neighbor joining method, based on sequence information.
Mentions: Phylogenetic analysis of NMT2 family reveals that it can be grouped into three major families (Figure 2). Group one family is composed of proteins from A. thaliana, the second family consists of R. norvegicus, H. sapiens, and B. Taurus, and the third family consists of M. musculus. The second family further subgrouped into R. norvegicus, H. sapiens, and B. taurus. The phylogenetic tree suggested that B. taurus belongs to the second group.

Bottom Line: Kinetic studies suggested that bovine brain NMT2 and human NMT1 show significant differences in their peptide substrate specificities.The metal ion Ca(2+) had stimulatory effects on NMT2 activity while Mn(2+) and Zn(2+) inhibited the enzyme activity.In addition, NMT2 activity was inhibited by various organic solvents and other detergents while NMT1 had a stimulatory effect.

View Article: PubMed Central - PubMed

Affiliation: Department of Pathology and Laboratory Medicine, College of Medicine and Health Research Division, Saskatchewan Cancer Agency, University of Saskatchewan, SK, Canada.

ABSTRACT
Protein N-myristoylation is a lipidic modification which refers to the covalent attachment of myristate, a 14-carbon saturated fatty acid, to the N-terminal glycine residue of a number of mammalian, viral, and fungal proteins. In this paper, we have cloned the gene coding for myristoyl-CoA:protein N-myristoyltransferase (NMT) from Bos tarus brain. The open reading frame codes for a 410-amino-acid protein and overexpressed in Escherichia coli. Kinetic studies suggested that bovine brain NMT2 and human NMT1 show significant differences in their peptide substrate specificities. The metal ion Ca(2+) had stimulatory effects on NMT2 activity while Mn(2+) and Zn(2+) inhibited the enzyme activity. In addition, NMT2 activity was inhibited by various organic solvents and other detergents while NMT1 had a stimulatory effect. Biochemical characterization suggested that both forms of NMT have unique characteristics. Further analysis towards functional role NMT2 will lead the development of therapeutic target for the progression of various diseases such as cancer, cardiovascular diseases, and neurodegenerative diseases.

Show MeSH
Related in: MedlinePlus