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2.5.1.7: UDP-N-acetylglucosamine 1-carboxyvinyltransferase

This is an abbreviated version!
For detailed information about UDP-N-acetylglucosamine 1-carboxyvinyltransferase, go to the full flat file.

Word Map on EC 2.5.1.7

Reaction

phosphoenolpyruvate
+
UDP-N-acetyl-alpha-D-glucosamine
=
phosphate
+
UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine

Synonyms

enol-pyruvyltransferase, enolpyruvyl UDP-GlcNAc synthase, enoylpyruvate transferase, enoylpyruvatetransferase, EPT, More, MurA, MurA enzyme, MurA transferase, MurAA, MurZ, phosphoenolpyruvate-UDP-acetylglucosamine-3-enolpyruvyltransferase, phosphoenolpyruvate:UDP-2-acetamido-2-deoxy-D-glucose 2-enoyl-1-carboxyethyltransferase, phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine enolpyruvyltransferase, phosphoenolpyruvate:uridine-5'-diphospho-N-acetyl-2-amino-2-deoxyglucose-3-enolpyruvyltransferase, phosphopyruvate-uridine diphosphoacetylglucosamine pyruvatetransferase, pyruvate-UDP-acetylglucosamine transferase, pyruvate-uridine diphospho-N-acetyl-glucosamine transferase, pyruvate-uridine diphospho-N-acetylglucosamine transferase, pyruvatetransferase, phosphoenolpyruvate-uridine diphosphoacetylglucosamine, pyruvic-uridine diphospho-N-acetylglucosaminyltransferase, UDP-GlcNAc enolpyruvyl transferase, UDP-N-acetylglucosamine 1-carboxyvinyl transferase, UDP-N-acetylglucosamine 1-carboxyvinyl-transferase, UDP-N-acetylglucosamine 1-carboxyvinyltransferase, UDP-N-acetylglucosamine enolpyruvyl transferase, UDP-N-acetylglucosamine enolpyruvyle transferase, UDP-N-acetylglucosamine enolpyruvyltransferase, UDP-N-acetylglucosamine enoylpyruvyltransferase, UDP-N-acetylglucosamine-enolpyruvyl transferase, UDP-NAG enolpyruvyl transferase, UNAG enolpyruvyl transferase

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.7 UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Engineering

Engineering on EC 2.5.1.7 - UDP-N-acetylglucosamine 1-carboxyvinyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C115D
the mutant enzyme lacks the ability to react with phosphoenolpyruvate covalently
C115S
C251S
-
site-directed mutagenesis, Cys251 is not involved in the catalysis, unaltered biochemical properties
C354S
-
site-directed mutagenesis, Cys354 is not involved in the catalysis, unaltered biochemical properties
C381S
-
site-directed mutagenesis, Cys381 is not involved in the catalysis, unaltered biochemical properties
D305A
D305C
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity
D305E
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, 0.1% activity compared to the wild-type
D305H
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity, fosfomycin is not covalently attached to Cys115
K22V/R120K
no residual activity, heat capacity changes are markedly redcued
K22V/R120V
no residual activity
N23A
-
site-directed mutagenesis, reduced activity, 20fold higher apparent dissociation constant for fosfomycin compared to wild-type
N23S
-
site-directed mutagenesis, reduced activity, 200fold higher apparent dissociation constant for fosfomycin compared to wild-type
R120K
less than 0.05% of wild-type activity, heat capacity changes are markedly redcued
C251S
-
site-directed mutagenesis, Cys251 is not involved in the catalysis, unaltered biochemical properties
-
C354S
-
site-directed mutagenesis, Cys354 is not involved in the catalysis, unaltered biochemical properties
-
C381S
-
site-directed mutagenesis, Cys381 is not involved in the catalysis, unaltered biochemical properties
-
D305A
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity, fosfomycin is not covalently attached to Cys115
-
D305C
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity
-
D305E
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, 0.1% activity compared to the wild-type
-
K22E
-
site-directed mutagenesis, exchange of conserved Lys residue located near the active site and involved in substrate binding leading to conformational changes, shows less than 0.5% activity compared to the wild-type, altered UDP-GlcNAc binding, highly reduced formation of covalent adduct between active site Cys115 and phosphoenolpyruvate or inhibitor fosfomycin
-
K22R
-
site-directed mutagenesis, exchange of conserved Lys residue located near the active site and involved in substrate binding leading to conformational changes, shows less than 0.5% activity compared to the wild-type, slightly reduced formation of covalent adduct between active site Cys115 and phosphoenolpyruvate or inhibitor fosfomycin
-
K22V
-
site-directed mutagenesis, exchange of conserved Lys residue located near the active site and involved in substrate binding leading to conformational changes, shows less than 0.5% activity compared to the wild-type, reduced formation of covalent adduct between active site Cys115 and phosphoenolpyruvate or inhibitor fosfomycin
-
N23A
-
site-directed mutagenesis, reduced activity, 20fold higher apparent dissociation constant for fosfomycin compared to wild-type
-
N23S
-
site-directed mutagenesis, reduced activity, 200fold higher apparent dissociation constant for fosfomycin compared to wild-type
-
C120S
-
catalytically inactive
C115A
-
site-directed mutagenesis, overexpression in Escherichia coli, no activity
C115D
C115E
-
site-directed mutagenesis, overexpression in Escherichia coli, gains fosfomycin resistance, enhanced pH-dependency of the reaction, low activity
C115N
-
site-directed mutagenesis, overexpression in Escherichia coli, deamination of Asn115 to Asp115
C115S
-
site-directed mutagenesis, overexpression in Escherichia coli, no activity
C115A
-
site-directed mutagenesis, overexpression in Escherichia coli, no activity
-
C115D
-
site-directed mutagenesis, overexpression in Escherichia coli, gains fosfomycin resistance, forms only the phospholactyl-enzyme intermediate adduct, but no UDP-GlcNAc-phosphoenolpyruvate, higher kcat than the wild-type at pH 7.0, enhanced pH-dependency of the reaction
-
C115E
-
site-directed mutagenesis, overexpression in Escherichia coli, gains fosfomycin resistance, enhanced pH-dependency of the reaction, low activity
-
C115N
-
site-directed mutagenesis, overexpression in Escherichia coli, deamination of Asn115 to Asp115
-
C115S
-
site-directed mutagenesis, overexpression in Escherichia coli, no activity
-
C117D
C115D
-
mutant protein is functional and resistant to fosfomycin and inhibitors 2-[4-(2-hydroxyethyl)piperazin-1-yl]-6,7-dimethoxy-3,4-dihydronaphthalen-1(2H)-one and2-(4-methylpiperazin-1-yl)-3,4-dihydronaphthalen-1(2H)-one
D120C
the mutant shows resistance against fosfomycin
additional information