Literature summary for 2.1.1.297 extracted from

Yang, Z.; Shipman, L.; Zhang, M.; Anton, B.P.; Roberts, R.J.; Cheng, X.
Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase (2004), J. Mol. Biol., 340, 695-706.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular replacement based on the data of Thermotoga maritima enzyme, in complex with the methyl-donor product S-adenosyl-L-homocysteine. Enzyme HemK contains two domains: a putative substrate binding domain at the N-terminus consisting of a five helix bundle and a seven-stranded catalytic domain at the C-terminus that harbors the binding site for S-adenosyl-L-homocysteine. The two domains are linked by a beta-hairpin. The apparent hinge mobility of the two domains may reflect functional importance during the reaction cycle	Escherichia coli

Crystallization (Comment)

Organism

molecular replacement based on the data of Thermotoga maritima enzyme, in complex with the methyl-donor product S-adenosyl-L-homocysteine. Enzyme HemK contains two domains: a putative substrate binding domain at the N-terminus consisting of a five helix bundle and a seven-stranded catalytic domain at the C-terminus that harbors the binding site for S-adenosyl-L-homocysteine. The two domains are linked by a beta-hairpin. The apparent hinge mobility of the two domains may reflect functional importance during the reaction cycle

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ACC1	-	-

Synonyms

Synonyms	Comment	Organism
HemK	-	Escherichia coli

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Release 2023.1 (January 2023)