Protein N-terminal methyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.1.1.244 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Protein N-terminal methyltransferase (EC 2.1.1.244, NMT1 (gene), METTL11A (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:N-terminal-(A,P,S)PK-(protein) methyltransferase. [1] [2] This enzyme catalyses the following chemical reaction
This enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys.
Methyltransferases are a large group of enzymes that all methylate their substrates but can be split into several subclasses based on their structural features. The most common class of methyltransferases is class I, all of which contain a Rossmann fold for binding S-Adenosyl methionine (SAM). Class II methyltransferases contain a SET domain, which are exemplified by SET domain histone methyltransferases, and class III methyltransferases, which are membrane associated. Methyltransferases can also be grouped as different types utilizing different substrates in methyl transfer reactions. These types include protein methyltransferases, DNA/RNA methyltransferases, natural product methyltransferases, and non-SAM dependent methyltransferases. SAM is the classical methyl donor for methyltransferases, however, examples of other methyl donors are seen in nature. The general mechanism for methyl transfer is a SN2-like nucleophilic attack where the methionine sulfur serves as the leaving group and the methyl group attached to it acts as the electrophile that transfers the methyl group to the enzyme substrate. SAM is converted to S-Adenosyl homocysteine (SAH) during this process. The breaking of the SAM-methyl bond and the formation of the substrate-methyl bond happen nearly simultaneously. These enzymatic reactions are found in many pathways and are implicated in genetic diseases, cancer, and metabolic diseases. Another type of methyl transfer is the radical S-Adenosyl methionine (SAM) which is the methylation of unactivated carbon atoms in primary metabolites, proteins, lipids, and RNA.
Histone-arginine N-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:histone-arginine Nomega-methyltransferase. This enzyme catalyses the following chemical reaction
In enzymology, a [cytochrome c]-arginine N-methyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a [cytochrome c]-lysine N-methyltransferase (EC 2.1.1.59) is an enzyme that catalyzes the chemical reaction
In enzymology, a [cytochrome-c]-methionine S-methyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a dimethylhistidine N-methyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a protein-glutamate O-methyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a protein-histidine N-methyltransferase is an enzyme that catalyzes the chemical reaction
The isoprenylcysteine o-methyltransferase carries out carboxyl methylation of cleaved eukaryotic proteins that terminate in a CaaX motif. In Saccharomyces cerevisiae this methylation is carried out by Ste14p, an integral endoplasmic reticulum membrane protein. Ste14p is the founding member of the isoprenylcysteine carboxyl methyltransferase (ICMT) family, whose members share significant sequence homology.
Uroporphyrinogen-III C-methyltransferase, uroporphyrinogen methyltransferase, uroporphyrinogen-III methyltransferase, adenosylmethionine-uroporphyrinogen III methyltransferase, S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase, uroporphyrinogen-III methylase, SirA, CysG, CobA, uroporphyrin-III C-methyltransferase, S-adenosyl-L-methionine:uroporphyrin-III C-methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:uroporphyrinogen-III C-methyltransferase. This enzyme catalyses the following chemical reaction
Glycine/sarcosine/dimethylglycine N-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:glycine(or sarcosine or N,N-dimethylglycine) N-methyltransferase . This enzyme catalyses the following chemical reaction
Methyl halide transferase is an enzyme with systematic name S-adenosylmethionine:iodide methyltransferase. This enzyme catalyses the following chemical reaction
Tricin synthase is an enzyme with systematic name S-adenosyl-L-methionine:tricetin 3',5'-O-dimethyltransferase. This enzyme catalyses the following chemical reaction
23S rRNA (adenine1618-N6)-methyltransferase (EC 2.1.1.181, rRNA large subunit methyltransferase F, YbiN protein, rlmF (gene), m6A1618 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine1618-N6)-methyltransferase. This enzyme catalyses the following chemical reaction
TRNA (adenine22-N1)-methyltransferase (EC 2.1.1.217, TrmK, YqfN, Sp1610 (gene), tRNA: m1A22 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (adenine22-N1)-methyltransferase. This enzyme catalyses the following chemical reaction
(phosphatase 2A protein)-leucine-carboxy methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:(phosphatase 2A protein)-leucine O-methyltransferase. This enzyme catalyses the following chemical reaction
Erythromycin 3''-O-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:erythromycin C 3''-O-methyltransferase. This enzyme catalyses the following chemical reaction
[Fructose-bisphosphate aldolase]-lysine N-methyltransferase (EC 2.1.1.259) is an enzyme that catalyses the following chemical reaction
Squalene methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:squalene C-methyltransferase. This enzyme catalyses the following chemical reaction
Botryococcene C-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:botryococcene C-methyltransferase.