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Literature summary for 1.13.11.2 extracted from

  • Hupert-Kocurek, K.; Wojcieszylska, D.; Guzik, U.
    Activity of a carboxyl-terminal truncated form of catechol 2,3-dioxygenase from Planococcus sp. S5 (2014), Sci. World J., 2014, 598518 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.13.11.2

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Planococcus sp. S5

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.09774
-
 catechol wild type enzyme, at pH 7.0 and 35°C Planococcus sp. S5

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
catechol + O2 Planococcus sp. S5 100% activity 2-hydroxymuconate-6-semialdehyde
-
 ?

Organism

Organism UniProt Comment Textmining
Planococcus sp. S5 E7DDG2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-methylcatechol + O2 6.12% activity compared to catechol Planococcus sp. S5 2-hydroxy-6-oxohepta-2,4-dienoate
-
 ?
4-chlorocatechol + O2 44.88% activity compared to catechol Planococcus sp. S5 4-chloro-2-hydroxymuconate semialdehyde
-
 ?
4-methylcatechol + O2 101.91% activity compared to catechol Planococcus sp. S5 2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
 ?
catechol + O2 100% activity Planococcus sp. S5 2-hydroxymuconate-6-semialdehyde
-
 ?

Synonyms

Synonyms Comment Organism
C23o
-
 Planococcus sp. S5

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
 Planococcus sp. S5

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Planococcus sp. S5