BRENDA - Enzyme Database show
show all sequences of 1.14.13.232

Identifying the minimal enzymes required for anhydrotetracycline biosynthesis

Zhang, W.; Watanabe, K.; Cai, X.; Jung, M.; Tang, Y.; Zhan, J.; J. Am. Chem. Soc. 130, 6068-6069 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Streptomyces rimosus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces rimosus
Q3S8Q4
bifunctional enzyme, hydroxylates 6-methylpretetramide at both the C-12a and C-4 positions, i.e. reactions of EC 1.14.13.232 and EC 1.14.1.3.233
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Streptomyces rimosus ATCC 10970
Q3S8Q4
bifunctional enzyme, hydroxylates 6-methylpretetramide at both the C-12a and C-4 positions, i.e. reactions of EC 1.14.13.232 and EC 1.14.1.3.233
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Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6-methylpretetramide + NADPH + H+ + O2
-
738445
Streptomyces rimosus
4-hydroxy-6-methylpretetramide + NADP+ + H2O
-
-
-
?
6-methylpretetramide + NADPH + H+ + O2
-
738445
Streptomyces rimosus ATCC 10970
4-hydroxy-6-methylpretetramide + NADP+ + H2O
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Streptomyces rimosus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Streptomyces rimosus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Streptomyces rimosus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6-methylpretetramide + NADPH + H+ + O2
-
738445
Streptomyces rimosus
4-hydroxy-6-methylpretetramide + NADP+ + H2O
-
-
-
?
6-methylpretetramide + NADPH + H+ + O2
-
738445
Streptomyces rimosus ATCC 10970
4-hydroxy-6-methylpretetramide + NADP+ + H2O
-
-
-
?
General Information
General Information
Commentary
Organism
physiological function
OxyL is a NADPH-dependent dioxygenase that hydroxylates 6-methylpretetramide at both C12a and C4 positions
Streptomyces rimosus
General Information (protein specific)
General Information
Commentary
Organism
physiological function
OxyL is a NADPH-dependent dioxygenase that hydroxylates 6-methylpretetramide at both C12a and C4 positions
Streptomyces rimosus
Other publictions for EC 1.14.13.232
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)
738050
Wang
Identification of oxyE as an a ...
Streptomyces rimosus, Streptomyces rimosus ATCC 10970
ChemBioChem
10
1544-1550
2009
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738445
Zhang
Identifying the minimal enzyme ...
Streptomyces rimosus, Streptomyces rimosus ATCC 10970
J. Am. Chem. Soc.
130
6068-6069
2008
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