Structural highlights
Function
NMT_CANAL Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Substrate specificity requires an N-terminal glycine in the nascent polypeptide substrates. Ser is present at position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6. Basic residues are preferred at positions 7 and 8.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Wiegand RC, Carr C, Minnerly JC, Pauley AM, Carron CP, Langner CA, Duronio RJ, Gordon JI. The Candida albicans myristoyl-CoA:protein N-myristoyltransferase gene. Isolation and expression in Saccharomyces cerevisiae and Escherichia coli. J Biol Chem. 1992 Apr 25;267(12):8591-8. PMID:1569105
- ↑ Lodge JK, Johnson RL, Weinberg RA, Gordon JI. Comparison of myristoyl-CoA:protein N-myristoyltransferases from three pathogenic fungi: Cryptococcus neoformans, Histoplasma capsulatum, and Candida albicans. J Biol Chem. 1994 Jan 28;269(4):2996-3009. PMID:8300631
- ↑ McWherter CA, Rocque WJ, Zupec ME, Freeman SK, Brown DL, Devadas B, Getman DP, Sikorski JA, Gordon JI. Scanning alanine mutagenesis and de-peptidization of a Candida albicans myristoyl-CoA:protein N-myristoyltransferase octapeptide substrate reveals three elements critical for molecular recognition. J Biol Chem. 1997 May 2;272(18):11874-80. PMID:9115247
