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Background
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N-myristoyltransferase (NMT) catalyzes the reaction of N-terminal myristoylation of many signaling proteins. It transfers myristic acid from myristoyl coenzyme A to the amino group of a protein's N-terminal glycine residue. Biochemical evidence indicates the presence of several distinct NMTs, varying in apparent molecular weight and /or subcellular distribution. The predicted 498-amino acid of human NMT2 protein shares 77% and 96% sequence identity with human NMT1 and mouse Nmt2 comprise two distinct families of N-myristoyltransferases.
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Background
References
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- Lindwasser, O.W., et al., Proc. Natl. Acad. Sci. U.S.A. 99(20):13037-13042 (2002).
- Kolluri, S.K., et al., Cancer Res. 61(23):8534-8539 (2001).
- Shiraishi, T., et al., Biochem. Biophys. Res. Commun. 282(5):1201-1205 (2001).
- Ono, A., et al., J. Virol. 73(5):4136-4144 (1999).
- Paillart, J.C., et al., J. Virol. 73(4):2604-2612 (1999).
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