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Literature summary for 6.3.3.3 extracted from

  • Yang, G.; Sandalova, T.; Lohman, K.; Lindqvist, Y.; Rendina, A.R.
    Active site mutants of the Escherichia coli dethiobiotin synthetase: effects of mutations on enzyme catalytic and structural properties (1997), Biochemistry, 36, 4751-4760.
    View publication on PubMed
Search for more literature for 6.3.3.3

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray crystallographic studies of the mutant enzymes S41A, S41C, K37Q, and K37L, show that the crystals are essentially isomorphous to that of the wild-type DTBS Escherichia coli

Protein Variants

Protein Variants Comment Organism
T11V active site mutant enzymes: T11V, E12A, E12D, K15Q, K37L, K37Q, K37R, S41A, S41C, T11V mutant shows a 24000fold increase in the Km for ATP with little or no change in the Km for 7,8-diaminononanoate and in turnover number. Mutants E12A and E12D show wild-type activity with slightly elevated turnover numbers. Unlike wild-type enzyme mutant enzyme E12A has the same apparent Km at subsaturating and saturating ATP concentrations. Mutant enzymes K15Q, K37Q, and K37R have no catalytic activity. Mutant enzymes S41A and S41C have the same turnover number as the wild-type enzyme and a moderate increase in Km for ATP and 7,8-diaminononanoate Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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 active site mutant enzymes: T11V, E12A, E12D, K15Q, K37L, K37Q, K37R, S41A, S41C, overproduced in Escherichia coli strain lacking a functional endogenous DTBS
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Purification (Commentary)

Purification (Comment) Organism
active site mutant enzymes: T11V, E12A, E12D, K15Q, K37L, K37Q, K37R, S41A, S41C, overproduced in Escherichia coli Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 7,8-diaminononanoate + CO2
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 Escherichia coli ADP + phosphate + dethiobiotin
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