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Literature summary for 1.14.12.15 extracted from

  • Fukuhara, Y.; Kasai, D.; Katayama, Y.; Fukuda, M.; Masai, E.
    Enzymatic properties of terephthalate 1,2-dioxygenase of Comamonas sp. strain E6 (2008), Biosci. Biotechnol. Biochem., 72, 2335-2341.
    View publication on PubMed
Search for more literature for 1.14.12.15

Cloned(Commentary)

Cloned (Comment) Organism
His-tag fused tphA1II and His-tag fused tphA2IIA3II genes expressed in Escherichia coli BL21(DE3) harboring pET-16tpa1 and pET-16tpa23 respectively, under the control of the T7 promoter Comamonas sp.

Inhibitors

Inhibitors Comment Organism Structure
EDTA 100% inhibition of TphA2IIA3II, Fe2+ restores activity, whereas Co2+, Cu2+, Mg2+, Mn2+, or Zn2+ can not restore activtiy Comamonas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
 NADPH
-
 Comamonas sp.
0.051
-
 NADH
-
 Comamonas sp.
0.072
-
 terephthalate at 30°C Comamonas sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ is required for activity Comamonas sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
17000
-
 2 * 48000, SDS-PAGE, TphA2II + 2 * 17000, SDS-PAGE, TphA3II. 2 * 48763, sequence analysis, TphA2II + 2 * 17236, sequence analysis, TphA3II Comamonas sp.
17236
-
 2 * 48000, SDS-PAGE, TphA2II + 2 * 17000, SDS-PAGE, TphA3II. 2 * 48763, sequence analysis, TphA2II + 2 * 17236, sequence analysis, TphA3II Comamonas sp.
37000
-
 1 * 37000, SDS-PAGE, TphA1II. 1 x 38861, sequence analysis, TphA1II Comamonas sp.
40000
-
 gel filtration, TphA1II Comamonas sp.
48000
-
 2 * 48000, SDS-PAGE, TphA2II + 2 * 17000, SDS-PAGE, TphA3II. 2 * 48763, sequence analysis, TphA2II + 2 * 17236, sequence analysis, TphA3II Comamonas sp.
48763
-
 2 * 48000, SDS-PAGE, TphA2II + 2 * 17000, SDS-PAGE, TphA3II. 2 * 48763, sequence analysis, TphA2II + 2 * 17236, sequence analysis, TphA3II Comamonas sp.
130000
-
 gel filtration and native-PAGE, TphA3II Comamonas sp.
140000
-
 gel filtration and native-PAGE, TphA2II Comamonas sp.

Organism

Organism UniProt Comment Textmining
Comamonas sp.
-
-
-
Comamonas sp. E6
-
-
-

Purification (Commentary)

Purification (Comment) Organism
to near homogeneity by Ni affinity chromatography Comamonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information does not catalyze phthalate, isophthalate, hydrobenzoate, protocatechuate, gallate, syringate, vanillate, benzoate, and 4-chlorobenzoate Comamonas sp. ?
-
 ?
additional information does not catalyze phthalate, isophthalate, hydrobenzoate, protocatechuate, gallate, syringate, vanillate, benzoate, and 4-chlorobenzoate Comamonas sp. E6 ?
-
 ?
terephthalate + NAD(P)H + O2 + H+ TPADO is specific for terephthalate Comamonas sp. (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD(P)+
-
 ?
terephthalate + NAD(P)H + O2 + H+ TPADO is specific for terephthalate Comamonas sp. E6 (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD(P)+
-
 ?
terephthalate + NADH + O2 + H+
-
 Comamonas sp. (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
-
 ?
terephthalate + NADH + O2 + H+
-
 Comamonas sp. E6 (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
-
 ?

Subunits

Subunits Comment Organism
heterotetramer 2 * 48000, SDS-PAGE, TphA2II + 2 * 17000, SDS-PAGE, TphA3II. 2 * 48763, sequence analysis, TphA2II + 2 * 17236, sequence analysis, TphA3II Comamonas sp.
monomer 1 * 37000, SDS-PAGE, TphA1II. 1 x 38861, sequence analysis, TphA1II Comamonas sp.

Synonyms

Synonyms Comment Organism
TPA 1,2-dioxygenase
-
 Comamonas sp.
TPADO
-
 Comamonas sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Comamonas sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
15
-
 about 60% of maximum TPADO activity, whereas activity is completely lost at 50°C Comamonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Comamonas sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
9
-
 about 20% of maximum TPADO activity, whereas activity is completely lost at pH 5 Comamonas sp.

Cofactor

Cofactor Comment Organism Structure
FAD TphA1II contains 0.7 mol of FAD/mol of protein, it binds one FAD molecule per monomer Comamonas sp.
NADH
-
 Comamonas sp.
NADPH preference for NADPH over NADH Comamonas sp.

General Information

General Information Comment Organism
physiological function TPADO is a two-component enzyme that consists of the termial oxygenase component TphA2IIA3II and the reductase component TphA1II Comamonas sp.