Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to tetrahydrotyrosine in Bacillus subtilis
Mahlstedt, S.A.; Walsh, C.T.; Biochemistry 49, 912-923 (2010) 
Data extracted from this reference:
Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Escherichia coli
Bacillus subtilis
General Stability
General Stability
Organism
unstable without glycerol in storage buffer
Bacillus subtilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
Bacillus subtilis
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
(3Z)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
-
-
?
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
Bacillus subtilis 168
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
(3Z)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Bacillus subtilis
P39639
-
-
Bacillus subtilis 168
P39639
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Bacillus subtilis
Reaction
Reaction
Commentary
Organism
Reaction ID
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate = 3-[(1E,4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
(2)
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
729204
Bacillus subtilis
(3Z)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
-
-
-
?
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate also undergoes a nonenzymatic isomerization
729204
Bacillus subtilis
(3Z)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
-
-
-
?
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
729204
Bacillus subtilis 168
(3Z)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
-
-
-
?
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate also undergoes a nonenzymatic isomerization
729204
Bacillus subtilis 168
(3Z)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
BacB
-
Bacillus subtilis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Bacillus subtilis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Bacillus subtilis
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Bacillus subtilis
General Stability (protein specific)
General Stability
Organism
unstable without glycerol in storage buffer
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
Bacillus subtilis
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
(3Z)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
-
-
?
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
Bacillus subtilis 168
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
(3Z)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
729204
Bacillus subtilis
(3Z)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
-
-
-
?
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate also undergoes a nonenzymatic isomerization
729204
Bacillus subtilis
(3Z)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
-
-
-
?
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
729204
Bacillus subtilis 168
(3Z)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
-
-
-
?
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate also undergoes a nonenzymatic isomerization
729204
Bacillus subtilis 168
(3Z)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Bacillus subtilis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Bacillus subtilis
General Information
General Information
Commentary
Organism
physiological function
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
Bacillus subtilis
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
Bacillus subtilis
Other publictions for EC 5.3.3.19
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)
729047
Wu
Bacilysin from Bacillus amylol ...
Bacillus amyloliquefaciens
Appl. Environ. Microbiol.
80
7512-7520
2014
-
-
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-
-
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-
-
-
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1
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2
2
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729211
Parker
Olefin isomerization regiochem ...
Bacillus subtilis, Bacillus subtilis 168
Biochemistry
51
3241-3251
2012
-
-
1
-
-
-
-
-
-
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-
6
-
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1
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-
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4
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1
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1
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1
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-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
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-
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729215
Parker
Stereochemical outcome at four ...
Bacillus subtilis, Bacillus subtilis 168
Biochemistry
51
5622-5632
2012
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1
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1
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6
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1
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4
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1
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1
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1
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-
4
-
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728865
Rajavel
Analysis of multiple crystal f ...
Bacillus subtilis, Bacillus subtilis 168
Acta Crystallogr. Sect. D
66
635-639
2010
-
-
1
1
-
-
-
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1
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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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1
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1
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-
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-
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-
1
1
-
-
-
729204
Mahlstedt
Investigation of anticapsin bi ...
Bacillus subtilis, Bacillus subtilis 168
Biochemistry
49
912-923
2010
-
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1
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1
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-
-
-
-
2
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6
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1
1
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4
-
1
1
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1
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1
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1
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2
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1
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4
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1
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1
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1
1
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729968
Rajavel
Role of Bacillus subtilis BacB ...
Bacillus subtilis, Bacillus subtilis 168
J. Biol. Chem.
284
31882-31892
2009
-
-
2
2
1
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-
1
-
1
-
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7
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2
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-
-
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4
-
2
2
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1
2
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-
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-
2
-
2
1
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1
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1
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2
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4
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2
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1
2
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1
1
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