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Literature summary for 2.5.1.55 extracted from

  • Xu, X.; Kona, F.; Wang, J.; Lu, J.; Stemmler, T.; Gatti, D.L.
    The catalytic and conformational cycle of Aquifex aeolicus KDO8P synthase: role of the L7 loop (2005), Biochemistry, 44, 12434-12444.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray structure of wild-type enzyme shows that when both phosphoenolpyruvate and D-arabinose 5-phosphate bind, the active site becomes isolated from the environment due to a conformational change of the L7 loop. The structures of the R106G mutant, without substrates, and with phosphoenolpyruvate and phosphoenolpyruvate plus D-arabinose 5-phosphate bound reveal that in R106G closure of the L7 loop is impaired Aquifex aeolicus

Protein Variants

Protein Variants Comment Organism
R106G the closure of the L7 loop is impaired. The mutant enzyme shows a smaller KM-value for phosphoenolpyruvate, larger Ki-value and KM-value for D-arabinose 5-phosphate and smaller Ki-values for phosphate and 2-dehydro-3-deoxy-D-octonate 8-phosphate compared ti wild-type enzyme Aquifex aeolicus

Inhibitors

Inhibitors Comment Organism Structure
2-dehydro-3-deoxy-D-octonate 8-phosphate mutant enzyme R106G is more severely inhibited than wild-type enzyme Aquifex aeolicus
D-arabinose 5-phosphate mutant enzyme R106G is less severely inhibited than wild-type enzyme Aquifex aeolicus
phosphate mutant enzyme R106G is more severely inhibited than wild-type enzyme Aquifex aeolicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Aquifex aeolicus

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus O66496
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + D-arabinose 5-phosphate
-
Aquifex aeolicus 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
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Synonyms

Synonyms Comment Organism
Kdo8P synthase
-
Aquifex aeolicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.32
-
phosphoenolpyruvate mutant enzyme R106G Aquifex aeolicus
0.32
-
D-arabinose 5-phosphate mutant enzyme R1096G Aquifex aeolicus
0.48
-
phosphoenolpyruvate wild-type enzyme Aquifex aeolicus
0.48
-
D-arabinose 5-phosphate wild-type enzyme Aquifex aeolicus