1.1.1.305: UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)

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For detailed information about UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating), go to the full flat file.

Reaction

Synonyms

ArnA, ArnA dehydrogenase, ArnADH, RsU4kpxs, UDP-alpha-D-xylose synthase, UDP-GlcUA dehydrogenase, UGA decarboxylase, UXS

ECTree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.1.305 UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)

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1	Activating Compound
2511	AA Sequence
2	Application
5	Cloned(Commentary)
9	Cofactor
6	Crystallization (Commentary)
3	General Information
2	kcat/KM [mM/s]
14	KM Value [mM]
1	Molecular Weight [Da]
10	Natural Substrates/ Products (Substrates)
10	Organism
3	Pathway
16	PDB ID
6	pH Optimum
1	pH Range
6	Protein Variants
3	Purification (Commentary)
1	Reaction
10	Reference
15	Substrates and Products (Substrate)
12	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
1	Temperature Range [°C]
2	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.1.1.305 - UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)

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crystal structure analysis, PDB entry 1Z7E

Escherichia coli

724362

crystal structure of the ArnA decarboxylase domain

Escherichia coli

P77398

696203

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

P77398

698732

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

P77398

701248

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

Escherichia coli

P77398

739796

purified recombinant UXS85-420 lacking the N-terminal membrane-spanning domain, hanging drop vapor diffusion method, precipitant containing 1.3 M ammonium sulfate, 0.1 M magnesium formate, and 0.15% PEG at 26°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement

Homo sapiens

724362