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Literature summary for 1.1.1.22 extracted from

  • Beattie, N.R.; Keul, N.D.; Hicks Sirmans, T.N.; McDonald, W.E.; Talmadge, T.M.; Taujale, R.; Kannan, N.; Wood, Z.A.
    Conservation of atypical allostery in C. elegans UDP-glucose dehydrogenase (2019), ACS omega, 4, 16318-16329 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of unliganded and UDP-xylose bound UGDH. The A109P substitution that differs human and Caenorhabditis elgans enzymes is accommodated by an Asn-to-Ser substitution at position 290. The allosteric transition is conserved in UGDH, and UDP-Xyl binding induces formation of the Eomega hexamer. The enzyme also exhibits hysteresis in progress curves and negative cooperativity with respect to NAD+ binding Caenorhabditis elegans

Inhibitors

Inhibitors Comment Organism Structure
UDP-xylose
-
Caenorhabditis elegans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.055
-
UDP-alpha-D-glucose Hill coefficient 1, pH 7.5, 25°C Caenorhabditis elegans
0.333
-
NAD+ K0.5 value, Hill coefficient 0.8, pH 7.5, 25°C Caenorhabditis elegans

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans Q19905
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-alpha-D-glucose + 2 NAD+ + H2O
-
Caenorhabditis elegans UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
?

Synonyms

Synonyms Comment Organism
sqv-4
-
Caenorhabditis elegans
UGDH
-
Caenorhabditis elegans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.23
-
UDP-alpha-D-glucose pH 7.5, 25°C Caenorhabditis elegans
1.7
-
NAD+ Hill coefficient 0.8, pH 7.5, 25°C Caenorhabditis elegans

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0069
-
UDP-xylose pH 7.5, 25°C Caenorhabditis elegans