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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
additional information
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
F4SGI5
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
ArnA is a key enzyme in the 4-amino-4-deoxy-L-arabinose-lipid A modification pathway. It is a bifunctional enzyme catalyzing the oxidative decarboxylation of UDP-glucuronic acid to the UDP-4''-ketopentose (UDP-beta-L-threo-pentapyranosyl-4''-ulose) and the N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-L-arabinose. The transformylase activity of the Escherichia coli ArnA is contained in its 300 N-terminal residues
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
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bi-functional enzyme, the oxidative decarboxylation of UDP-glucuronic acid is catalyzed by the 345-residue C-terminal domain of ArnA. The 304-residue N-terminal domain catalyzes the N-10-formyltetrahydrofolate-dependent formylation of the 4''-amine of UDP-4-amino-4-deoxy-L-arabinose, generating the sugar nucleotide, uridine 5'-diphospho-beta-(4-deoxy-4-formamido-L-arabinose). The two domains of ArnA are expressed independently as active proteins in Escherichia coli. Both are required for maintenance of polymyxin resistance and L-4-amino-4-deoxy-L-arabinose modification of lipid A. Only the formylated sugar nucleotide is converted in vitro to an undecaprenyl phosphate-linked form by the enzyme ArnC
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-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
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
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ArnA is a bi-functional enzyme. The oxidative decarboxylation of UDP-glucuronic acid is catalyzed by the 345-residue C-terminal domain of ArnA. The 304-residue N-terminal domain catalyzes the N-10-formyltetrahydrofolate-dependent formylation of the 4''-amine of UDP-L-4-amino-4-deoxy-L-arabinose, generating the sugar nucleotide, uridine 5'-diphospho-beta-(4-deoxy-4-formamido-L-arabinose)
the major isomer is the cis-formamido rotamer
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
ArnA is a key enzyme in the 4-amino-4-deoxy-L-arabinose-lipid A modification pathway. It is a bifunctional enzyme catalyzing the oxidative decarboxylation of UDP-glucuronic acid to the UDP-4''-ketopentose (UDP-beta-L-threo-pentapyranosyl-4''-ulose) and the N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-L-arabinose. The transformylase activity of the Escherichia coli ArnA is contained in its 300 N-terminal residues. A mechanism for the transformylation reaction is proposed, catalyzed by ArnA involving residues N102, H104, and D140
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-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
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
F4SGI5
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additional information
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F4SGI5
the bifunctional enzyme has N- and C-terminal domains catalyzing formylation and oxidative decarboxylation reactions, respectively
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additional information
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F4SGI5
the bifunctional enzyme has N- and C-terminal domains catalyzing formylation and oxidative decarboxylation reactions, respectively
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
F4SGI5
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
ArnA is a key enzyme in the 4-amino-4-deoxy-L-arabinose-lipid A modification pathway. It is a bifunctional enzyme catalyzing the oxidative decarboxylation of UDP-glucuronic acid to the UDP-4''-ketopentose (UDP-beta-L-threo-pentapyranosyl-4''-ulose) and the N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-L-arabinose. The transformylase activity of the Escherichia coli ArnA is contained in its 300 N-terminal residues
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
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bi-functional enzyme, the oxidative decarboxylation of UDP-glucuronic acid is catalyzed by the 345-residue C-terminal domain of ArnA. The 304-residue N-terminal domain catalyzes the N-10-formyltetrahydrofolate-dependent formylation of the 4''-amine of UDP-4-amino-4-deoxy-L-arabinose, generating the sugar nucleotide, uridine 5'-diphospho-beta-(4-deoxy-4-formamido-L-arabinose). The two domains of ArnA are expressed independently as active proteins in Escherichia coli. Both are required for maintenance of polymyxin resistance and L-4-amino-4-deoxy-L-arabinose modification of lipid A. Only the formylated sugar nucleotide is converted in vitro to an undecaprenyl phosphate-linked form by the enzyme ArnC
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-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
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
F4SGI5
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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°
hanging drop vapor diffusion method, crystal structure of the ArnA transformylase domain is solved to 1.7 A resolution
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
N-formyltransferase domain of the enzyme in complex with N5-formyltetrahydrofolate and UDP-4-amino-4-deoxy-beta-L-arabinopyranose, hanging drop vapor diffusion method, using 20-22% poly(ethyleneglycol) 5000, 50 mM MgCl2, 100 mM HEPES (pH 8.0) at 21°C
F4SGI5
structure of apo-ArnA and comparison with its ATP- and UDP-glucuronic acid-bound counterparts. In the crystal structure, a binding pocket at the centre of each ArnA trimer in its apo state pocket is occupied by a dithiothreitol molecule. Formation of the pocket is linked to a cascade of structural rearrangements that emerge from the NAD+-binding site. A small effector molecule is postulated that binds to the central pocket and modulates the catalytic properties of ArnA
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Gatzeva-Topalova, P.Z.; May, A.P.; Sousa, M.C.
Crystal structure and mechanism of the Escherichia coli ArnA (PmrI) transformylase domain. An enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance
Biochemistry
44
5328-5338
2005
Escherichia coli (P77398)
brenda
Breazeale, S.D.; Ribeiro, A.A.; Raetz, C.R.
Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid a species modified with 4-amino-4-deoxy-L-arabinose
J. Biol. Chem.
277
2886-2896
2001
Escherichia coli (P77398)
brenda
Breazeale, S.D.; Ribeiro, A.A.; McClerren, A.L.; Raetz, C.R.
A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-Amino-4-deoxy-L-arabinose. Identification and function oF UDP-4-deoxy-4-formamido-L-arabinose
J. Biol. Chem.
280
14154-14167
2005
Escherichia coli
brenda
Williams, G.J.; Breazeale, S.D.; Raetz. C.R.; Naismith. J.H.
Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis
J. Biol. Chem.
280
23000-23008
2005
Escherichia coli (P77398)
brenda
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.
Structure
13
929-942
2005
Escherichia coli (P77398)
brenda
Fischer, U.; Hertlein, S.; Grimm, C.
The structure of apo ArnA features an unexpected central binding pocket and provides an explanation for enzymatic cooperativity
Acta Crystallogr. Sect. D
71
687-696
2015
Escherichia coli (P77398)
brenda
Han, S.H.; Kim, B.G.; Yoon, J.A.; Chong, Y.; Ahn, J.H.
Synthesis of flavonoid O-pentosides by Escherichia coli through engineering of nucleotide sugar pathways and glycosyltransferase
Appl. Environ. Microbiol.
80
2754-2762
2014
Escherichia coli (A0A140N587)
brenda
Sonawane, K.; Parulekar, R.; Malkar, R.; Nimbalkar, P.; Barage, S.; Jadhav, D.
Homology modeling and molecular docking studies of ArnA protein from Erwinia amylovora role in polymyxin antibiotic resistance
J. Plant Biochem. Biotechnol.
24
425-432
2015
Erwinia amylovora
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brenda
Genthe, N.A.; Thoden, J.B.; Holden, H.M.
Structure of the Escherichia coli ArnA N-formyltransferase domain in complex with N5-formyltetrahydrofolate and UDP-Ara4N
Protein Sci.
25
1555-1562
2016
Escherichia coli (F4SGI5), Escherichia coli W3110 (F4SGI5)
brenda