BRENDA - Enzyme Database
show all sequences of 6.3.2.10

Conditionally lethal Escherichia coli murein mutants contain point defects that map to regions conserved among murein and folyl poly-g-glutamate ligases: identification of a ligase superfamily

Eveland, S.S.; Pompliano, D.L.; Anderson, M.S.; Biochemistry 36, 6223-6229 (1997)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression of naturally occuring mutant allele murF2 with A288T mutation as glutathione S-transferase fusion protein; expression of point mutants, expression of wild-type and naturally occuring mutant allele murF2 with A288T mutation as glutathione S-transferase fusion proteins
Escherichia coli
Engineering
Protein Variants
Commentary
Organism
A288T
naturally occuring murF2 allele, expressed as a fusion protein with glutathione S-transferase, is 181fold less catalytically active than the wild-type enzyme at 30°c and even more reduced at 42°C
Escherichia coli
E158A
site-directed mutagenesis, 4520fold reduced activity compared to the wild-type
Escherichia coli
E158D
site-directed mutagenesis, 246fold reduced activity compared to the wild-type
Escherichia coli
E158G
site-directed mutagenesis, over 451fold reduced activity compared to the wild-type
Escherichia coli
H188A
site-directed mutagenesis, 203fold reduced activity compared to the wild-type
Escherichia coli
H188D
site-directed mutagenesis, 2990fold reduced activity compared to the wild-type
Escherichia coli
H188G
site-directed mutagenesis, 214fold reduced activity compared to the wild-type
Escherichia coli
H188N
site-directed mutagenesis, 1860fold reduced activity compared to the wild-type
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala-D-Ala
Escherichia coli
-
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala
-
Escherichia coli
?
ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala-D-Ala
Escherichia coli
part of bacterial peptidoglycan biosynthesis
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala
-
Escherichia coli
?
additional information
Escherichia coli
the specific activity of the mutant enzyme is highly reduced compared to the wild-type murF
?
-
Escherichia coli
?
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
P11880
gene murF; naturally occuring mutant murF2 allele, with A288T exchange
-
Reaction
Reaction
Commentary
Organism
Reaction ID
ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
ordered kinetic mechanism, E158 and H188 are critical for enzyme activity
Escherichia coli
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.04
-
purified recombinant enzyme, 42°C; purified recombinant murF2 mutant, 42°C
Escherichia coli
0.062
-
purified recombinant enzyme, 30°C; purified recombinant murF2 mutant, 30°C
Escherichia coli
11.2
-
purified recombinant wild-type enzyme, 30°C
Escherichia coli
13.9
-
purified recombinant wild-type enzyme, 42°C
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala-D-Ala
-
649829
Escherichia coli
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala
-
649829
Escherichia coli
?
ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala-D-Ala
formation of an acyl phosphate intermediate
649829
Escherichia coli
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala
-
649829
Escherichia coli
?
ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala-D-Ala
part of bacterial peptidoglycan biosynthesis
649829
Escherichia coli
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala
-
649829
Escherichia coli
?
additional information
the specific activity of the mutant enzyme is highly reduced compared to the wild-type murF
649829
Escherichia coli
?
-
649829
Escherichia coli
?
Synonyms
Synonyms
Commentary
Organism
D-Ala-D-Ala-adding enzyme
-
Escherichia coli
More
member of ligase superfamily
Escherichia coli
Synthetase, uridine diphosphoacetylmuramoylpentapeptide
-
Escherichia coli
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine synthetase
-
Escherichia coli
UDP-N-acetylmuramoylalanyl-D-glutamyl-lysine-D-alanyl-D-alanine ligase
-
Escherichia coli
UDPacetylmuramoylpentapeptide synthetase
-
Escherichia coli
Uridine diphosphoacetylmuramoylpentapeptide synthetase
-
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
-
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of naturally occuring mutant allele murF2 with A288T mutation as glutathione S-transferase fusion protein; expression of point mutants, expression of wild-type and naturally occuring mutant allele murF2 with A288T mutation as glutathione S-transferase fusion proteins
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
-
Escherichia coli
Engineering (protein specific)
Protein Variants
Commentary
Organism
A288T
naturally occuring murF2 allele, expressed as a fusion protein with glutathione S-transferase, is 181fold less catalytically active than the wild-type enzyme at 30°c and even more reduced at 42°C
Escherichia coli
E158A
site-directed mutagenesis, 4520fold reduced activity compared to the wild-type
Escherichia coli
E158D
site-directed mutagenesis, 246fold reduced activity compared to the wild-type
Escherichia coli
E158G
site-directed mutagenesis, over 451fold reduced activity compared to the wild-type
Escherichia coli
H188A
site-directed mutagenesis, 203fold reduced activity compared to the wild-type
Escherichia coli
H188D
site-directed mutagenesis, 2990fold reduced activity compared to the wild-type
Escherichia coli
H188G
site-directed mutagenesis, 214fold reduced activity compared to the wild-type
Escherichia coli
H188N
site-directed mutagenesis, 1860fold reduced activity compared to the wild-type
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala-D-Ala
Escherichia coli
-
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala
-
Escherichia coli
?
ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala-D-Ala
Escherichia coli
part of bacterial peptidoglycan biosynthesis
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala
-
Escherichia coli
?
additional information
Escherichia coli
the specific activity of the mutant enzyme is highly reduced compared to the wild-type murF
?
-
Escherichia coli
?
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.04
-
purified recombinant enzyme, 42°C; purified recombinant murF2 mutant, 42°C
Escherichia coli
0.062
-
purified recombinant enzyme, 30°C; purified recombinant murF2 mutant, 30°C
Escherichia coli
11.2
-
purified recombinant wild-type enzyme, 30°C
Escherichia coli
13.9
-
purified recombinant wild-type enzyme, 42°C
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala-D-Ala
-
649829
Escherichia coli
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala
-
649829
Escherichia coli
?
ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala-D-Ala
formation of an acyl phosphate intermediate
649829
Escherichia coli
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala
-
649829
Escherichia coli
?
ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala-D-Ala
part of bacterial peptidoglycan biosynthesis
649829
Escherichia coli
ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala
-
649829
Escherichia coli
?
additional information
the specific activity of the mutant enzyme is highly reduced compared to the wild-type murF
649829
Escherichia coli
?
-
649829
Escherichia coli
?
Other publictions for EC 6.3.2.10
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743956
An
Purification, crystallization ...
Acinetobacter baumannii, Acinetobacter baumannii AB307-0294
Acta Crystallogr. Sect. F
70
976-978
2014
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1
1
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1
1
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4
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1
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1
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2
2
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744222
Cha
ATP-binding mode including a ...
Acinetobacter baumannii, Acinetobacter baumannii AB307-0294
Biochem. Biophys. Res. Commun.
450
1045-1050
2014
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1
1
1
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1
1
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2
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3
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1
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6
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3
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1
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6
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1
1
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701735
Baum
MurF inhibitors with antibacte ...
Escherichia coli
Antimicrob. Agents Chemother.
53
3240-3247
2009
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702541
Sova
Phosphorylated hydroxyethylami ...
Escherichia coli
Bioorg. Chem.
37
217-222
2009
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1
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702636
Turk
Discovery of new inhibitors of ...
Escherichia coli
Bioorg. Med. Chem.
17
1884-1889
2009
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1
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681042
Khedkar
Design of inhibitors of the Mu ...
Streptococcus pneumoniae
J. Chem. Inf. Model.
47
1839-1846
2007
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31
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1
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1
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22
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22
31
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677589
Baum
Utility of muropeptide ligase ...
Escherichia coli
Antimicrob. Agents Chemother.
50
230-236
2006
-
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1
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3
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3
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3
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679177
Stamper
Structure-based optimization o ...
Streptococcus pneumoniae
Chem. Biol. Drug Des.
67
58-65
2006
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1
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1
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6
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680459
Sobral
Role of murF in cell wall bios ...
Staphylococcus aureus
J. Bacteriol.
188
2543-2553
2006
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680941
Comess
An ultraefficient affinity-bas ...
Streptococcus pneumoniae
J. Biomol. Screen.
11
743-754
2006
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1
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4
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661790
Serina
Glycopeptide resistance determ ...
Actinoplanes teichomyceticus
FEMS Microbiol. Lett.
240
69-74
2004
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651110
Dementin
Evidence of a functional requi ...
Escherichia coli
Eur. J. Biochem.
268
5800-5807
2001
6
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8
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17
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17
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649111
Yan
Crystallization and preliminar ...
Escherichia coli, Escherichia coli K37
Acta Crystallogr. Sect. D
55
2033-2034
1999
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649829
Eveland
Conditionally lethal Escherich ...
Escherichia coli
Biochemistry
36
6223-6229
1997
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1
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8
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1
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4
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7
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8
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986
Parquet
Nucleotide sequence of the mur ...
Escherichia coli
Nucleic Acids Res.
17
5379
1989
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987
Walsh
Enzymes in the D-alanine branc ...
Escherichia coli
J. Biol. Chem.
264
2393-2396
1989
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984
Oppenheim
Formation of D-alanyl-D-alanin ...
Enterococcus faecalis, Staphylococcus aureus
FEBS Lett.
48
172-175
1974
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2
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4
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985
Linnett
Cell wall polymers of Bacillus ...
Lysinibacillus sphaericus, Lysinibacillus sphaericus 9602
J. Bacteriol.
120
342-354
1974
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