BRENDA - Enzyme Database
show all sequences of 4.2.99.20

Exploiting the high-resolution crystal structure of Staphylococcus aureus MenH to gain insight into enzyme activity

Dawson, A.; Fyfe, P.; Gillet, F.; Hunter, W.; BMC Struct. Biol. 11, 19 (2011)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Escherichia coli
Staphylococcus aureus
Crystallization (Commentary)
Crystallization (Commentary)
Organism
to 2 A resolution. The overall basic active site displays pronounced hydrophobic character on one side and these properties complement those of the substrate. A complex network of hydrogen bonds involving well-ordered water molecules serves to position key residues participating in the recognition of substrate and subsequent catalysis. Proton shuttle mechanism, reliant on a catalytic triad consisting of Ser89, Asp216 and His243. The reaction is initiated by proton abstraction from the substrate by an activated Ser89. The propensity to form a conjugated system provides the driving force for pyruvate elimination. During the elimination, a methylene group is converted to a methyl and probybly His243 provides a proton, previously acquired from Ser89 for reduction. A conformational change of the protonated His243 may be encouraged by the presence of an anionic intermediate in the active site
Staphylococcus aureus
Organism
Organism
UniProt
Commentary
Textmining
Staphylococcus aureus
A0A0H2WW38
-
-
Synonyms
Synonyms
Commentary
Organism
MenH
-
Staphylococcus aureus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Staphylococcus aureus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
to 2 A resolution. The overall basic active site displays pronounced hydrophobic character on one side and these properties complement those of the substrate. A complex network of hydrogen bonds involving well-ordered water molecules serves to position key residues participating in the recognition of substrate and subsequent catalysis. Proton shuttle mechanism, reliant on a catalytic triad consisting of Ser89, Asp216 and His243. The reaction is initiated by proton abstraction from the substrate by an activated Ser89. The propensity to form a conjugated system provides the driving force for pyruvate elimination. During the elimination, a methylene group is converted to a methyl and probybly His243 provides a proton, previously acquired from Ser89 for reduction. A conformational change of the protonated His243 may be encouraged by the presence of an anionic intermediate in the active site
Staphylococcus aureus
Other publictions for EC
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)
730042
Sun
Molecular basis of the general ...
Escherichia coli
J. Biol. Chem.
289
15867-15879
2014
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1
1
7
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6
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1
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1
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1
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1
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5
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1
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1
7
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6
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1
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5
-
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6
6
730729
Johnston
Crystal structures of E. coli ...
Escherichia coli
PLoS ONE
8
e61325
2013
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1
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2
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1
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714632
Dawson
Exploiting the high-resolution ...
Staphylococcus aureus
BMC Struct. Biol.
11
19
2011
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1
1
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1
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702326
Jiang
Catalytic mechanism of SHCHC s ...
Escherichia coli
Biochemistry
48
6921-6931
2009
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1
-
12
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13
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1
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1
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1
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3
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13
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1
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12
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13
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1
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1
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13
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13
13
685225
Jiang
Identification and characteriz ...
Escherichia coli
Biochemistry
47
3426-3434
2008
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3
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10
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1
1
1
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4
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1
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3
1
4
1
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5
1
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3
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10
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1
1
1
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1
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3
1
1
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5
1
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1
1
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5
5
685086
Jiang
Menaquinone biosynthesis in Es ...
Escherichia coli K-12
Biochemistry
46
10979-10989
2007
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