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Literature summary for 1.1.1.305 extracted from

  • Gatzeva-Topalova, P.Z.; May, A.P.; Sousa, M.C.
    Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance. (2005), Structure, 13, 929-942.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, crystal structure of the full-length bifunctional ArnA with UDP-glucuronic acid and ATP bound to the dehydrogenase domain. Binding of UDP-glucuronic acid triggers a 17 A conformational change in ArnA_DH that opens the NAD+ binding site while trapping UDP-glucuronic acid Escherichia coli

Protein Variants

Protein Variants Comment Organism
R610M activity is 800fold lower than wild-type activity Escherichia coli
R619E no activity Escherichia coli
R619Y no activity Escherichia coli
S433A activity is 30fold lower than wild-type activity Escherichia coli
S433T no activity Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-glucuronate + NAD+ Escherichia coli the modification of lipid A with 4-amino-4-deoxy-L-arabinose allows gram-negative bacteria to resist the antimicrobial activity of cationic antimicrobial peptides and antibiotics such as polymyxin. ArnA is the first enzyme specific to the lipid A-Ara4N pathway. It contains two functionally and physically separable domains: a dehydrogenase domain (ArnA_DH) catalyzing the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid, and a transformylase domain that formylates UDP-4-amino-4-deoxy-L-arabinose UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P77398
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-glucuronate + NAD+ the modification of lipid A with 4-amino-4-deoxy-L-arabinose allows gram-negative bacteria to resist the antimicrobial activity of cationic antimicrobial peptides and antibiotics such as polymyxin. ArnA is the first enzyme specific to the lipid A-Ara4N pathway. It contains two functionally and physically separable domains: a dehydrogenase domain (ArnA_DH) catalyzing the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid, and a transformylase domain that formylates UDP-4-amino-4-deoxy-L-arabinose Escherichia coli UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
-
 ?
UDP-glucuronate + NAD+ ordered mechanism of substrate binding and product release is proposed. R619 functions as a general acid in catalysis Escherichia coli UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
ArnA dehydrogenase
-
 Escherichia coli
ArnADH
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Escherichia coli