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2.1.1.14: 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase

This is an abbreviated version!
For detailed information about 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.14

Reaction

5-methyltetrahydropteroyltri-L-glutamate
+
L-homocysteine
=
tetrahydropteroyltri-L-glutamate
 +
L-methionine

Synonyms

5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferase, AtMetE, cobalamin-independent methionine synthase, cobalamin-independent methionine synthase (MetE), homocysteine methylase, Met-8, MET1, Met6, Met6p, MetE, methionine synthase MetE, methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase, methyltransferase, tetrahydropteroylglutamate-homocysteine transmethylase, MS1, PpMetE, tetrahydropteroyltriglutamate methyltransferase, TM1286

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.14 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase

Engineering

Engineering on EC 2.1.1.14 - 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N126A
13% of wild-type activity
Y660A
no residual activity
Y660F
93% of wild-type activity
Y660Q
14% of wild-type activity
N126A
-
13% of wild-type activity
-
Y660A
-
no residual activity
-
Y660F
-
93% of wild-type activity
-
Y660Q
-
14% of wild-type activity
-
C645A
-
the mutation confers resistance to diamide when cells are grown in media lacking methionine, but not when cells are grown in the presence of methionine, cysteine 645 serves to modulate the activity of MetE in vivo in response to disulfide stress
C726S
-
mutant does not contain zinc, no activity, probably due to lack of zinc
V39A/R46C/T106I/K713E
mutant confers accelerated growth in the Escherichia coli K-12 WE strain in the presence of acetate. Strains harboring acetate-tolerant MetE mutants are less inhibited by homocysteine in L-isoleucine-enriched medium. The acetate-tolerant MetE mutants stimulate the growth of the host strain at elevated temperatures of 44 and 45°C. The mutant MetE enzymes display a reduced melting temperature but an enhanced in vivo stability
V39A/R46C/T106I/K713E/C645A
C645A mutation additionally improves acetate tolerance. Strains harboring acetate-tolerant MetE mutants are less inhibited by homocysteine in L-isoleucine-enriched medium. The acetate-tolerant MetE mutants stimulate the growth of the host strain at elevated temperatures of 44 and 45°C. The mutant MetE enzymes display a reduced melting temperature but an enhanced in vivo stability
D113R
mutation abrogate nuclear localization
R742A
nuclear localization is abrogated by the deletion of 107 C-terminal amino acids or the R742A mutation