BRENDA - Enzyme Database show
show all sequences of 2.1.1.281

In vitro characterization of enzymes involved in the synthesis of nonproteinogenic residue (2S,3S)-beta-methylphenylalanine in glycopeptide antibiotic mannopeptimycin

Huang, Y.T.; Lyu, S.Y.; Chuang, P.H.; Hsu, N.S.; Li, Y.S.; Chan, H.C.; Huang, C.J.; Liu, Y.C.; Wu, C.J.; Yang, W.B.; Li, T.L.; ChemBioChem 10, 2480-2487 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
His6-tagged enzyme is expressed in Escherichia coli
Streptomyces hygroscopicus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.014
-
S-adenosyl-L-methionine
pH 8.0, 30°C
Streptomyces hygroscopicus
2.5
-
2-oxo-3-phenylpropanoate
pH 8.0, 30°C
Streptomyces hygroscopicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + 2-oxo-3-phenylpropanoate
Streptomyces hygroscopicus
the enzyme is involved in synthesis of the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the glycopeptide antibiotic mannopeptimycin
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-methyl-3-phenylpropanoate
-
-
?
S-adenosyl-L-methionine + 2-oxo-3-phenylpropanoate
Streptomyces hygroscopicus NRRL3085
the enzyme is involved in synthesis of the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the glycopeptide antibiotic mannopeptimycin
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-methyl-3-phenylpropanoate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces hygroscopicus
-
-
-
Streptomyces hygroscopicus NRRL3085
-
-
-
Purification (Commentary)
Commentary
Organism
-
Streptomyces hygroscopicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + 2-oxo-3-phenylpropanoate
the enzyme is involved in synthesis of the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the glycopeptide antibiotic mannopeptimycin
722038
Streptomyces hygroscopicus
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-methyl-3-phenylpropanoate
-
-
-
?
S-adenosyl-L-methionine + 2-oxo-3-phenylpropanoate
2-oxo-3-phenylpropanoate i.e. 3-phenylpyruvate. S-Adenosyl-L-methionine has higher binding affinity for the enzyme than 2-oxo-3-phenylpropanoate, and the C-C bond formation in (3S)-2-oxo-3-methyl-3-phenylpropanoate might be the rate-limiting step, as opposed to the C-S bond breakage in S-adenosyl-L-methionine. No enzyme activity on glutamic acid, cinnamic acid, phenyl acetic acid and benzoyl acetic acid. The alpha-keto and beta-phenyl functional groups are crucial in MppJ molecular recognition. The enzyme strictly transfers a methyl group from S-adenosyl-L-methionine the beta position of 2-oxo-3-phenylpropanoate
722038
Streptomyces hygroscopicus
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-methyl-3-phenylpropanoate
(3S)-2-oxo-3-methyl-3-phenylpropanoate i.e. (3S)-beta-methyl-phenylpyruvate
-
-
?
S-adenosyl-L-methionine + 2-oxo-3-phenylpropanoate
the enzyme is involved in synthesis of the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the glycopeptide antibiotic mannopeptimycin
722038
Streptomyces hygroscopicus NRRL3085
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-methyl-3-phenylpropanoate
-
-
-
?
S-adenosyl-L-methionine + 2-oxo-3-phenylpropanoate
2-oxo-3-phenylpropanoate i.e. 3-phenylpyruvate. S-Adenosyl-L-methionine has higher binding affinity for the enzyme than 2-oxo-3-phenylpropanoate, and the C-C bond formation in (3S)-2-oxo-3-methyl-3-phenylpropanoate might be the rate-limiting step, as opposed to the C-S bond breakage in S-adenosyl-L-methionine. No enzyme activity on glutamic acid, cinnamic acid, phenyl acetic acid and benzoyl acetic acid. The alpha-keto and beta-phenyl functional groups are crucial in MppJ molecular recognition. The enzyme strictly transfers a methyl group from S-adenosyl-L-methionine the beta position of 2-oxo-3-phenylpropanoate
722038
Streptomyces hygroscopicus NRRL3085
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-methyl-3-phenylpropanoate
(3S)-2-oxo-3-methyl-3-phenylpropanoate i.e. (3S)-beta-methyl-phenylpyruvate
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.8
-
2-oxo-3-phenylpropanoate
pH 8.0, 30°C
Streptomyces hygroscopicus
8.15
-
S-adenosyl-L-methionine
pH 8.0, 30°C
Streptomyces hygroscopicus
Cloned(Commentary) (protein specific)
Commentary
Organism
His6-tagged enzyme is expressed in Escherichia coli
Streptomyces hygroscopicus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.014
-
S-adenosyl-L-methionine
pH 8.0, 30°C
Streptomyces hygroscopicus
2.5
-
2-oxo-3-phenylpropanoate
pH 8.0, 30°C
Streptomyces hygroscopicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + 2-oxo-3-phenylpropanoate
Streptomyces hygroscopicus
the enzyme is involved in synthesis of the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the glycopeptide antibiotic mannopeptimycin
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-methyl-3-phenylpropanoate
-
-
?
S-adenosyl-L-methionine + 2-oxo-3-phenylpropanoate
Streptomyces hygroscopicus NRRL3085
the enzyme is involved in synthesis of the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the glycopeptide antibiotic mannopeptimycin
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-methyl-3-phenylpropanoate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Streptomyces hygroscopicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + 2-oxo-3-phenylpropanoate
the enzyme is involved in synthesis of the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the glycopeptide antibiotic mannopeptimycin
722038
Streptomyces hygroscopicus
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-methyl-3-phenylpropanoate
-
-
-
?
S-adenosyl-L-methionine + 2-oxo-3-phenylpropanoate
2-oxo-3-phenylpropanoate i.e. 3-phenylpyruvate. S-Adenosyl-L-methionine has higher binding affinity for the enzyme than 2-oxo-3-phenylpropanoate, and the C-C bond formation in (3S)-2-oxo-3-methyl-3-phenylpropanoate might be the rate-limiting step, as opposed to the C-S bond breakage in S-adenosyl-L-methionine. No enzyme activity on glutamic acid, cinnamic acid, phenyl acetic acid and benzoyl acetic acid. The alpha-keto and beta-phenyl functional groups are crucial in MppJ molecular recognition. The enzyme strictly transfers a methyl group from S-adenosyl-L-methionine the beta position of 2-oxo-3-phenylpropanoate
722038
Streptomyces hygroscopicus
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-methyl-3-phenylpropanoate
(3S)-2-oxo-3-methyl-3-phenylpropanoate i.e. (3S)-beta-methyl-phenylpyruvate
-
-
?
S-adenosyl-L-methionine + 2-oxo-3-phenylpropanoate
the enzyme is involved in synthesis of the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the glycopeptide antibiotic mannopeptimycin
722038
Streptomyces hygroscopicus NRRL3085
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-methyl-3-phenylpropanoate
-
-
-
?
S-adenosyl-L-methionine + 2-oxo-3-phenylpropanoate
2-oxo-3-phenylpropanoate i.e. 3-phenylpyruvate. S-Adenosyl-L-methionine has higher binding affinity for the enzyme than 2-oxo-3-phenylpropanoate, and the C-C bond formation in (3S)-2-oxo-3-methyl-3-phenylpropanoate might be the rate-limiting step, as opposed to the C-S bond breakage in S-adenosyl-L-methionine. No enzyme activity on glutamic acid, cinnamic acid, phenyl acetic acid and benzoyl acetic acid. The alpha-keto and beta-phenyl functional groups are crucial in MppJ molecular recognition. The enzyme strictly transfers a methyl group from S-adenosyl-L-methionine the beta position of 2-oxo-3-phenylpropanoate
722038
Streptomyces hygroscopicus NRRL3085
S-adenosyl-L-homocysteine + (3S)-2-oxo-3-methyl-3-phenylpropanoate
(3S)-2-oxo-3-methyl-3-phenylpropanoate i.e. (3S)-beta-methyl-phenylpyruvate
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.8
-
2-oxo-3-phenylpropanoate
pH 8.0, 30°C
Streptomyces hygroscopicus
8.15
-
S-adenosyl-L-methionine
pH 8.0, 30°C
Streptomyces hygroscopicus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.32
-
2-oxo-3-phenylpropanoate
pH 8.0, 30°C
Streptomyces hygroscopicus
582
-
S-adenosyl-L-methionine
pH 8.0, 30°C
Streptomyces hygroscopicus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.32
-
2-oxo-3-phenylpropanoate
pH 8.0, 30°C
Streptomyces hygroscopicus
582
-
S-adenosyl-L-methionine
pH 8.0, 30°C
Streptomyces hygroscopicus
Other publictions for EC 2.1.1.281
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
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)
735362
Zou
Structure and mechanism of a n ...
Streptomyces hygroscopicus, Streptomyces hygroscopicus NRRL3085
Acta Crystallogr. Sect. D
70
1549-1560
2014
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1
1
5
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1
2
2
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3
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6
1
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5
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1
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2
2
-
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722038
Huang
In vitro characterization of e ...
Streptomyces hygroscopicus, Streptomyces hygroscopicus NRRL3085
ChemBioChem
10
2480-2487
2009
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4
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2
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1
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