Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.3.2.16: lipid II:glycine glycyltransferase

This is an abbreviated version!
For detailed information about lipid II:glycine glycyltransferase, go to the full flat file.

Reaction

N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-D-alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetyl-D-glucosamine
+
glycyl-tRNAGly
=
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetyl-D-glucosamine
 +
tRNAGly

Synonyms

FemX

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.16 lipid II:glycine glycyltransferase

Engineering

Engineering on EC 2.3.2.16 - lipid II:glycine glycyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F196L
26% of wild-type activity
F196Y
87% of wild-type activity
F305L
16% of wild-type activity
F305Y
98% of wild-type activity
G319S
13% of wild-type activity
G319V
5% of wild-type activity
K306A
8% of wild-type activity
K306C
38% of wild-type activity
K306N
9% of wild-type activity
K306R
25% of wild-type activity
Q144E
11% of wild-type activity
Q144T
79% of wild-type activity
Y216F
41% of wild-type activity
Y73F
40% of wild-type activity
Y73L
40% of wild-type activity
additional information
-
in strains carrying mutations of FemA, femAB, or the femAX genes, the sorting reaction of surface proteins is significantly slowed. Strains carrying mutations in the fem genes display a decreased rate of surface protein precursor cleavage as compared with the wild-type strains, suggesting that the altered cross-bridges slow the anchoring of surface proteins