BRENDA - Enzyme Database
show all sequences of 2.6.1.87

Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme

Noland, B.W.; Newman, J.M.; Hendle, J.; Badger, J.; Christopher, J.A.; Tresser, J.; Buchanan, M.D.; Wright, T.A.; Rutter, M.E.; Sanderson, W.E.; Muller-Dieckmann, H.J.; Gajiwala, K.S.; Buchanan, S.G.; Structure 10, 1569-1580 (2002) View publication on PubMed

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
hanging drop vapor diffusion method, high-resolution crystal structures are solved for two native forms and one covalently inhibited form of Salmonella typhimurium ArnB (crystal structure of ArnB aminotransferase with pyridomine 5'-phosphate, crystal structure of ArnB transferase with pyridoxal 5'-phosphate, crystal structure of ArnB aminotransferase with cycloserine and pyridoxal 5'-phosphate)
Salmonella enterica subsp. enterica serovar Typhimurium
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
Salmonella enterica subsp. enterica serovar Typhimurium
lipid A modification with 4-amino-4-deoxy-L-arabinose confers on certain pathogenic bacteria, such as Salmonella, resistance to cationic antimicrobial peptides, including those derived from the innate immune system ArnB catalysis of amino group transfer from glutamic acid to the 4''-position of a UDP-linked keto-pyranose molecule to form UDP-4-amino-4-deoxy-L-arabinose represents a key step in the lipid A modification pathway
UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
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-
r
Organism
Organism
UniProt
Commentary
Textmining
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Salmonella enterica subsp. enterica serovar Typhimurium
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
-
701247
Salmonella enterica subsp. enterica serovar Typhimurium
UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
-
-
-
r
UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
lipid A modification with 4-amino-4-deoxy-L-arabinose confers on certain pathogenic bacteria, such as Salmonella, resistance to cationic antimicrobial peptides, including those derived from the innate immune system ArnB catalysis of amino group transfer from glutamic acid to the 4''-position of a UDP-linked keto-pyranose molecule to form UDP-4-amino-4-deoxy-L-arabinose represents a key step in the lipid A modification pathway
701247
Salmonella enterica subsp. enterica serovar Typhimurium
UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
-
-
-
r
Cloned(Commentary) (protein specific)
Commentary
Organism
hanging drop vapor diffusion method, high-resolution crystal structures are solved for two native forms and one covalently inhibited form of Salmonella typhimurium ArnB (crystal structure of ArnB aminotransferase with pyridomine 5'-phosphate, crystal structure of ArnB transferase with pyridoxal 5'-phosphate, crystal structure of ArnB aminotransferase with cycloserine and pyridoxal 5'-phosphate)
Salmonella enterica subsp. enterica serovar Typhimurium
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
Salmonella enterica subsp. enterica serovar Typhimurium
lipid A modification with 4-amino-4-deoxy-L-arabinose confers on certain pathogenic bacteria, such as Salmonella, resistance to cationic antimicrobial peptides, including those derived from the innate immune system ArnB catalysis of amino group transfer from glutamic acid to the 4''-position of a UDP-linked keto-pyranose molecule to form UDP-4-amino-4-deoxy-L-arabinose represents a key step in the lipid A modification pathway
UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
-
Salmonella enterica subsp. enterica serovar Typhimurium
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
-
701247
Salmonella enterica subsp. enterica serovar Typhimurium
UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
-
-
-
r
UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
lipid A modification with 4-amino-4-deoxy-L-arabinose confers on certain pathogenic bacteria, such as Salmonella, resistance to cationic antimicrobial peptides, including those derived from the innate immune system ArnB catalysis of amino group transfer from glutamic acid to the 4''-position of a UDP-linked keto-pyranose molecule to form UDP-4-amino-4-deoxy-L-arabinose represents a key step in the lipid A modification pathway
701247
Salmonella enterica subsp. enterica serovar Typhimurium
UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate
-
-
-
r
Other publictions for EC 2.6.1.87
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)
698724
Breazeale
Origin of lipid A species modi ...
Escherichia coli
J. Biol. Chem.
278
24731-24739
2003
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701247
Noland
Structural studies of Salmonel ...
Salmonella enterica subsp. enterica serovar Typhimurium
Structure
10
1569-1580
2002
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