BRENDA - Enzyme Database
show all sequences of 1.14.13.200

Nucleotide sequences and heterologous expression of tcmG and tcmP, biosynthetic genes for tetracenomycin C in Streptomyces glaucescens

Decker, H.; Motamedi, H.; Hutchinson, C.R.; J. Bacteriol. 175, 3876-3886 (1993)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Streptomyces lividans
Streptomyces glaucescens
Organism
Organism
UniProt
Commentary
Textmining
Streptomyces glaucescens
P39888
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-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
tetracenomycin A2 + 2 O2 + 2 NAD(P)H + 2 H+
-
729909
Streptomyces glaucescens
tetracenomycin C + 2 NAD(P)+ + H2O
enzyme is responsible for the hydroxylation of tetracenomycin A2 at positions C-4, C-4a, and C-12a to give tetracenomycin C
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Streptomyces glaucescens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Streptomyces glaucescens
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Streptomyces lividans
Streptomyces glaucescens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
tetracenomycin A2 + 2 O2 + 2 NAD(P)H + 2 H+
-
729909
Streptomyces glaucescens
tetracenomycin C + 2 NAD(P)+ + H2O
enzyme is responsible for the hydroxylation of tetracenomycin A2 at positions C-4, C-4a, and C-12a to give tetracenomycin C
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Streptomyces glaucescens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Streptomyces glaucescens
General Information
General Information
Commentary
Organism
physiological function
enzyme is responsible for the hydroxylation of tetracenomycin A2 at positions C-4, C-4a, and C-12a to give tetracenomycin C, i.e. the final step in tetracenomycin C biosynthesis
Streptomyces glaucescens
General Information (protein specific)
General Information
Commentary
Organism
physiological function
enzyme is responsible for the hydroxylation of tetracenomycin A2 at positions C-4, C-4a, and C-12a to give tetracenomycin C, i.e. the final step in tetracenomycin C biosynthesis
Streptomyces glaucescens
Other publictions for EC 1.14.13.200
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)
730232
Rafanan
Cloning, sequencing, and heter ...
Streptomyces olivaceus, Streptomyces olivaceus Tue2353
J. Nat. Prod.
64
444-449
2001
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2
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728863
Beynon
Crystallization and preliminar ...
Streptomyces glaucescens
Acta Crystallogr. Sect. D
56
1647-1651
2000
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730547
Rafanan
Triple hydroxylation of tetrac ...
Streptomyces glaucescens, Streptomyces olivaceus, Streptomyces olivaceus Tue2353
Org. Lett.
2
3225-3227
2000
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2
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727813
Shen
Triple hydroxylation of tetrac ...
Streptomyces glaucescens
J. Biol. Chem.
269
30726-30733
1994
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5
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3
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3
1
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1
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729909
Decker
Nucleotide sequences and heter ...
Streptomyces glaucescens
J. Bacteriol.
175
3876-3886
1993
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