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Literature summary for 1.1.1.305 extracted from

  • Gatzeva-Topalova, P.Z.; May, A.P.; Sousa, M.C.
    Crystal structure of Escherichia coli ArnA (PmrI) decarboxylase domain. A key enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance (2005), Biochemistry, 43, 13370-13379.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.305

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the ArnA decarboxylase domain Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.054
-
 UDP-glucuronate pH 8.0, 37°C, C-terminal domain of ArnA Escherichia coli
0.086
-
 UDP-glucuronate pH 8.0, 37°C, full-length enzyme Escherichia coli
0.57
-
 NAD+ pH 8.0, 37°C, C-terminal domain of ArnA Escherichia coli
0.76
-
 NAD+ pH 8.0, 37°C, full-length enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-glucuronate + NAD+ Escherichia coli ArnA is a key enzyme in the lipid A modification pathway, and its deletion abolishes both the Ara4N-lipid A modification and polymyxin resistance. ArnA is a bifunctional enzyme. It can catalyze the NAD+-dependent decarboxylation of UDP-glucuronic acid to UDP-4-keto-arabinose and the N-10-formyltetrahydrofolate dependent formylation of 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
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-glucuronate + NAD+ ArnA is a key enzyme in the lipid A modification pathway, and its deletion abolishes both the Ara4N-lipid A modification and polymyxin resistance. ArnA is a bifunctional enzyme. It can catalyze the NAD+-dependent decarboxylation of UDP-glucuronic acid to UDP-4-keto-arabinose and the N-10-formyltetrahydrofolate dependent formylation of UDP-4-amino-4-deoxy-L-arabinose Escherichia coli UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
-
 ?
UDP-glucuronate + NAD+ ArnA is a bifunctional enzyme. It can catalyze the NAD+-dependent decarboxylation of UDP-glucuronic acid to UDP-4-keto-arabinose and the N-10-formyltetrahydrofolate dependent formylation of UDP-4-amino-4-deoxy-L-arabinose. The NAD+-dependent decarboxylating activity is contained in the 360 amino acid C-terminal domain of ArnA. This domain is separable from the N-terminal fragment, and its activity is identical to that of the full-length enzyme. T432, Y463, K467, R619, and S433 are involved in the mechanism of NAD+-dependent oxidation of the 4''-OH of the UDP-glucuronic acid and decarboxylation of the UDP-4-keto-glucuronic acid intermediate Escherichia coli UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Escherichia coli