BRENDA - Enzyme Database show
show all sequences of 1.14.19.57

Biosynthesis of polybrominated aromatic organic compounds by marine bacteria

Agarwal, V.; El Gamal, A.; Yamanaka, K.; Poth, D.; Kersten, R.; Schorn, M.; Allen, E.; Moore, B.; Nat. Chem. Biol. 10, 640-647 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Pseudoalteromonas luteoviolacea
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudoalteromonas luteoviolacea
-
-
-
Pseudoalteromonas luteoviolacea 2ta16
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + 3 FADH2 + 3 bromide + 3 O2
-
745834
Pseudoalteromonas luteoviolacea
3,4,5-tribromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + 3 FAD + 6 H2O
-
-
-
?
1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2
-
745834
Pseudoalteromonas luteoviolacea
5-bromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O
-
-
-
?
4,5-dibromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2
-
745834
Pseudoalteromonas luteoviolacea
3,4,5-tribromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O
-
-
-
?
5-bromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2
-
745834
Pseudoalteromonas luteoviolacea
4,5-dibromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Pseudoalteromonas luteoviolacea
NADPH
-
Pseudoalteromonas luteoviolacea
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Pseudoalteromonas luteoviolacea
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Pseudoalteromonas luteoviolacea
NADPH
-
Pseudoalteromonas luteoviolacea
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + 3 FADH2 + 3 bromide + 3 O2
-
745834
Pseudoalteromonas luteoviolacea
3,4,5-tribromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + 3 FAD + 6 H2O
-
-
-
?
1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2
-
745834
Pseudoalteromonas luteoviolacea
5-bromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O
-
-
-
?
4,5-dibromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2
-
745834
Pseudoalteromonas luteoviolacea
3,4,5-tribromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O
-
-
-
?
5-bromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2
-
745834
Pseudoalteromonas luteoviolacea
4,5-dibromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O
-
-
-
?
General Information
General Information
Commentary
Organism
physiological function
deletion of gene Bmp2 abolishes the production of bromopyrroles. In the presence of Escherichia coli flavin reductase SsuE, NADPH and bromide, Bmp2 catalyzes the bromination of pyrrolyl-S-Bmp1(acyl carrier protein) to mono-, di- and tribromopyrrolyl-S-Bmp1(acyl carrier protein)
Pseudoalteromonas luteoviolacea
General Information (protein specific)
General Information
Commentary
Organism
physiological function
deletion of gene Bmp2 abolishes the production of bromopyrroles. In the presence of Escherichia coli flavin reductase SsuE, NADPH and bromide, Bmp2 catalyzes the bromination of pyrrolyl-S-Bmp1(acyl carrier protein) to mono-, di- and tribromopyrrolyl-S-Bmp1(acyl carrier protein)
Pseudoalteromonas luteoviolacea
Other publictions for EC 1.14.19.57
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)
745834
Agarwal
Biosynthesis of polybrominate ...
Pseudoalteromonas luteoviolacea, Pseudoalteromonas luteoviolacea 2ta16
Nat. Chem. Biol.
10
640-647
2014
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