BRENDA - Enzyme Database show
show all sequences of 2.1.2.13

Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis

Williams, G.J.; Breazeale, S.D.; Raetz. C.R.; Naismith. J.H.; J. Biol. Chem. 280, 23000-23008 (2005)

Data extracted from this reference:

Application
Application
Commentary
Organism
medicine
modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. L-Ara4N biosynthesis is therefore a potential anti-infective target
Escherichia coli
Cloned(Commentary)
Commentary
Organism
overexpression of native and selenomethionine decarboxylase and formyltransferase domains of ArnA
Escherichia coli
Crystallization (Commentary)
Crystallization
Organism
crystallization of native and Se-Met decarboxylase protein. Good quality crystals are obtained with a precipitant solution of 3.2 M NaCl, 0.1 M Bistris, pH 5.2, using a drop containing 0.004 ml of protein and 0.004 ml of precipitant equilibrated against a reservoir of 0.1 ml of precipitant. Space group as P4(1)3(2), with cell dimensions a = b = c = 149.4 A, beta = gamma = 90°
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
E434Q
mutant is inactive, suggesting that chemical rather than steric properties of this residue are crucial in the decarboxylation reaction
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
Escherichia coli
modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. The bifunctional enzyme ArnA is required for 4-amino-4-deoxy-L-arabinose biosynthesis and catalyzes the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid to generate a UDP-4'-keto-pentose sugar and also catalyzes transfer of a formyl group from N-10-formyltetrahydrofolate to the 4'-amine of UDP-4-amino-4-deoxy-L-arabinose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P77398
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. The bifunctional enzyme ArnA is required for 4-amino-4-deoxy-L-arabinose biosynthesis and catalyzes the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid to generate a UDP-4'-keto-pentose sugar and also catalyzes transfer of a formyl group from N-10-formyltetrahydrofolate to the 4'-amine of UDP-4-amino-4-deoxy-L-arabinose
698732
Escherichia coli
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
-
-
-
?
10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. The bifunctional enzyme ArnA is required for 4-amino-4-deoxy-L-arabinose biosynthesis and catalyzes the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid to generate a UDP-4'-keto-pentose sugar and also catalyzes transfer of a formyl group from N-10-formyltetrahydrofolate to the 4'-amine of UDP-4-amino-4-deoxy-L-arabinose. The active site of formyltransfer in ArnA includes the key catalytic residues Asn102, His104, and Asp140
698732
Escherichia coli
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli
Application (protein specific)
Application
Commentary
Organism
medicine
modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. L-Ara4N biosynthesis is therefore a potential anti-infective target
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpression of native and selenomethionine decarboxylase and formyltransferase domains of ArnA
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystallization of native and Se-Met decarboxylase protein. Good quality crystals are obtained with a precipitant solution of 3.2 M NaCl, 0.1 M Bistris, pH 5.2, using a drop containing 0.004 ml of protein and 0.004 ml of precipitant equilibrated against a reservoir of 0.1 ml of precipitant. Space group as P4(1)3(2), with cell dimensions a = b = c = 149.4 A, beta = gamma = 90°
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E434Q
mutant is inactive, suggesting that chemical rather than steric properties of this residue are crucial in the decarboxylation reaction
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
Escherichia coli
modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. The bifunctional enzyme ArnA is required for 4-amino-4-deoxy-L-arabinose biosynthesis and catalyzes the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid to generate a UDP-4'-keto-pentose sugar and also catalyzes transfer of a formyl group from N-10-formyltetrahydrofolate to the 4'-amine of UDP-4-amino-4-deoxy-L-arabinose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. The bifunctional enzyme ArnA is required for 4-amino-4-deoxy-L-arabinose biosynthesis and catalyzes the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid to generate a UDP-4'-keto-pentose sugar and also catalyzes transfer of a formyl group from N-10-formyltetrahydrofolate to the 4'-amine of UDP-4-amino-4-deoxy-L-arabinose
698732
Escherichia coli
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
-
-
-
?
10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. The bifunctional enzyme ArnA is required for 4-amino-4-deoxy-L-arabinose biosynthesis and catalyzes the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid to generate a UDP-4'-keto-pentose sugar and also catalyzes transfer of a formyl group from N-10-formyltetrahydrofolate to the 4'-amine of UDP-4-amino-4-deoxy-L-arabinose. The active site of formyltransfer in ArnA includes the key catalytic residues Asn102, His104, and Asp140
698732
Escherichia coli
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
-
-
-
?
Other publictions for EC 2.1.2.13
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)
739796
Fischer
The structure of apo ArnA feat ...
Escherichia coli
Acta Crystallogr. Sect. D
71
687-696
2015
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739902
Han
Synthesis of flavonoid O-pento ...
Escherichia coli
Appl. Environ. Microbiol.
80
2754-2762
2014
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696208
Gatzeva-Topalova
Crystal structure and mechanis ...
Escherichia coli
Biochemistry
44
5328-5338
2005
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698730
Breazeale
A formyltransferase required f ...
Escherichia coli
J. Biol. Chem.
280
14154-14167
2005
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698732
Williams
Structure and function of both ...
Escherichia coli
J. Biol. Chem.
280
23000-23008
2005
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701248
Gatzeva-Topalova
Structure and mechanism of Arn ...
Escherichia coli
Structure
13
929-942
2005
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698723
Breazeale
Oxidative decarboxylation of U ...
Escherichia coli
J. Biol. Chem.
277
2886-2896
2001
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