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ligand binding properties of the NMT/ACBD6 complex can explain how the NMT reaction can proceed in the presence of the very abundant competitive substrate, C(16)-CoA.
induction of NMT2 may play a central role in dioxin carcinogenicity.
NMT1 (show NMT1 Proteins) and NMT2 have only partially overlapping functions; NMT1 (show NMT1 Proteins) is critical for tumor cell proliferation
Protein-protein interaction of NMTs revealed that m-calpain (show CAPN2 Proteins) interacts with NMT1 (show NMT1 Proteins) while caspase-3 (show CASP3 Proteins) interacts with NMT2.
Disruption of the gene for NMT2 by a t(8;10) translocation in a male with hypogonadism.
Nef is preferentially myristoylated by NMT2, suggesting that selective inhibition of NMT2 may provide a novel means of blocking HIV virulence.
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.
, glycylpeptide N-tetradecanoyltransferase 2-like
, NMT 2
, glycylpeptide N-tetradecanoyltransferase 2
, glycylpeptide N-tetradecanoyltransferase 2 variant 3
, myristoyl-CoA:protein N-myristoyltransferase 2
, peptide N-myristoyltransferase 2
, type II N-myristoyltransferase