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Literature summary for 1.1.1.305 extracted from

  • Polizzi, S.J.; Walsh, R.M.; Peeples, W.B.; Lim, J.M.; Wells, L.; Wood, Z.A.
    Human UDP-?-D-xylose synthase and Escherichia coli ArnA conserve a conformational shunt that controls whether xylose or 4-keto-xylose is produced (2012), Biochemistry, 51, 8844-8855.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
NAD+ exogenous NAD+ stimulates enzyme activity, because a small fraction of hUXS releases the NADH and UDP-alpha-D-4-dehydroxylose intermediates as products during turnover. The resulting apoenzyme can be rescued by exogenous NAD+, explaining the apparent stimulatory effect of added cofactor Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis, PDB entry 1Z7E Escherichia coli
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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetics of decarboxylation reaction, overview Escherichia coli
additional information
-
additional information steady-state kinetics of decarboxylation reaction, overview Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli UGA decarboxylase produces NADH and UDP-alpha-D-4-dehyroxylose as products, it can rebind NADH and UDP-alpha-D-4-dehyroxylose to slowly make UDP-alpha-D-xylose ?
-
?
UDP-alpha-D-glucuronate + NAD+ Escherichia coli
-
UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
-
r
UDP-alpha-D-glucuronate + NAD+ Homo sapiens
-
UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information UGA decarboxylase produces NADH and UDP-alpha-D-4-dehyroxylose as products, it can rebind NADH and UDP-alpha-D-4-dehyroxylose to slowly make UDP-alpha-D-xylose Escherichia coli ?
-
?
additional information hUXS contains a bound NAD+ cofactor that it recycles by first oxidizing UDP-alpha-D-glucuronic acid, and then reducing the UDP-alpha-D-4-dehydroxylose to produce UDP-alpha-D-xylose Homo sapiens ?
-
?
UDP-alpha-D-glucuronate + NAD+
-
Escherichia coli UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
-
r
UDP-alpha-D-glucuronate + NAD+
-
Homo sapiens UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
-
r

Synonyms

Synonyms Comment Organism
ArnA
-
Escherichia coli
UDP-alpha-D-xylose synthase
-
Homo sapiens
UGA decarboxylase
-
Escherichia coli
UXS
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli
25
-
assay at Homo sapiens

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
additional information induced-fit conformational change associated with cofactor binding, overview Escherichia coli
NAD+
-
Escherichia coli
NAD+ NAD+ is buried in the enzyme core catalytic domain, binding structure, overview Homo sapiens
NADH
-
Escherichia coli

General Information

General Information Comment Organism
evolution the enzyme is a member of the short-chain dehydrogenase/reductase family of nucleotide-sugar modifying enzymes Homo sapiens
additional information induced-fit conformational change associated with cofactor binding, overview Escherichia coli