Literature summary for 2.1.1.297 extracted from

Schubert, H.L.; Phillips, J.D.; Hill, C.P.
Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine AdoMet-dependent methyltransferase (2003), Biochemistry, 42, 5592-5599.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Thermotoga maritima

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 2.2 A resolution. The C-terminal domain of PrmC adopts the canonical S-adenosyl-L-methionine-dependent methyltransferase fold and shares structural similarity with the nucleotide N-methyltransferases in the active site, including use of a conserved (D/N)PPY motif to select and position the glutamine substrate. Residues of the PrmC 197NPPY200 motif form hydrogen bonds that position the planar Gln side chain such that the lone-pair electrons on the nitrogen nucleophile are oriented toward the methyl group of S-adenosyl-Lmethionine. In the product complex, the methyl group remains pointing toward the sulfur, consistent with either an sp3-hybridized, positively charged Gln nitrogen, or a neutral sp2-hybridized nitrogen in a strained conformation. Due to steric overlap within the active site, proton loss and formation of the neutral planar methylamide product are likely to occur during or after product release	Thermotoga maritima

Crystallization (Comment)

Organism

to 2.2 A resolution. The C-terminal domain of PrmC adopts the canonical S-adenosyl-L-methionine-dependent methyltransferase fold and shares structural similarity with the nucleotide N-methyltransferases in the active site, including use of a conserved (D/N)PPY motif to select and position the glutamine substrate. Residues of the PrmC 197NPPY200 motif form hydrogen bonds that position the planar Gln side chain such that the lone-pair electrons on the nitrogen nucleophile are oriented toward the methyl group of S-adenosyl-Lmethionine. In the product complex, the methyl group remains pointing toward the sulfur, consistent with either an sp3-hybridized, positively charged Gln nitrogen, or a neutral sp2-hybridized nitrogen in a strained conformation. Due to steric overlap within the active site, proton loss and formation of the neutral planar methylamide product are likely to occur during or after product release

Thermotoga maritima

Organism

Organism	UniProt	Comment	Textmining
Thermotoga maritima	Q9WYV8	-	-
Thermotoga maritima DSM 3109	Q9WYV8	-	-

Synonyms

Synonyms	Comment	Organism
PrmC/HemK	-	Thermotoga maritima
release factor glutamine methyltransferase	-	Thermotoga maritima

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Release 2023.1 (January 2023)