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Literature summary for 4.2.1.41 extracted from

  • Taberman, H.; Andberg, M.; Parkkinen, T.; Jänis, J.; Penttilä, M.; Hakulinen, N.; Koivula, A.; Rouvinen, J.
    Structure and function of a decarboxylating Agrobacterium tumefaciens keto-deoxy-D-galactarate dehydratase (2014), Biochemistry, 53, 8052-8060 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Agrobacterium fabrum

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of keto-deoxy-d-galactarate dehydratase and its complexes with pyruvate and 2-oxoadipic acid, two substrate analogues, are determined to 1.7 A, 1.5 A, and 2.1 A resolution, respectively Agrobacterium fabrum
crystals are grown by the hanging drop vapor diffusion method at 20°C, crystal structures are determined to 1.7 A, 1.5 A, and 2.1 A resolution, respectively Agrobacterium fabrum

Protein Variants

Protein Variants Comment Organism
S211A the specific activity of the purified Ser211Ala mutant enzyme is approximately 30 times lower than the activity of the wild-type enzyme Agrobacterium fabrum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.5
-
5-dehydro-4-deoxy-D-glucarate pH 7.5, 22°C Agrobacterium fabrum

Organism

Organism UniProt Comment Textmining
Agrobacterium fabrum Q8UB77
-
-
Agrobacterium fabrum ATCC 33970 Q8UB77
-
-
Agrobacterium fabrum C58 Q8UB77
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Agrobacterium fabrum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-dehydro-4-deoxy-D-glucarate i.e. 3-deoxy-L-threo-2-hexulosarate Agrobacterium fabrum 2,5-dioxopentanoate + CO2
-
?
5-dehydro-4-deoxy-D-glucarate i.e. 3-deoxy-L-threo-2-hexulosarate Agrobacterium fabrum C58 2,5-dioxopentanoate + CO2
-
?
5-dehydro-4-deoxy-D-glucarate i.e. 3-deoxy-L-threo-2-hexulosarate Agrobacterium fabrum ATCC 33970 2,5-dioxopentanoate + CO2
-
?

Synonyms

Synonyms Comment Organism
KDG dehydratase
-
Agrobacterium fabrum
keto-deoxy-D-galactarate dehydratase
-
Agrobacterium fabrum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
the enzyme retains more than 60% of its activity after 22 h Agrobacterium fabrum
50
-
activity is reduced to 20% after 22 h Agrobacterium fabrum
70
-
less than 1% activity is detected after 30 min Agrobacterium fabrum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
8.83
-
5-dehydro-4-deoxy-D-glucarate pH 7.5, 22°C Agrobacterium fabrum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8
-
Agrobacterium fabrum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
17
-
5-dehydro-4-deoxy-D-glucarate pH 7.5, 22°C Agrobacterium fabrum