Disease relevance of 3-Methyl-1, 2-dihydroxybenzene

• With 3-methylcatechol as substrate, the ratio of intradiol and extradiol cleavage activities of Pseudomonas pyrocatechase during purification was almost constant and was about 17 [1].
• In aqueous media, 10 mM of 3-methylcatechol was produced and production was limited by 3-methylcatechol toxicity to the biocatalyst [2].
• MhqB was also overexpressed in E. coli, and the purified enzyme showed an extradiol ring cleavage activity toward 3-methylcatechol but a very low activity was observed toward 4-methylcatechol [3].

High impact information on 3-Methyl-1, 2-dihydroxybenzene

• The bacterium, Oxy6, was also able to oxidize o-xylene and the xylene monooxygenase (XMO) pathway intermediate 3-methylcatechol [4].
• From o-cresol, the I100Q saturation mutagenesis mutant and the M180T/E284G DNA shuffling mutant formed methylhydroquinone (0.50 and 0.19 nmol/min/mg of protein, respectively) and 3-methylcatechol (0.49 and 1.5 nmol/min/mg of protein, respectively) [5].
• The amount of 3-methylcatechol produced in an aliphatic alcohol/water bioreactor was 10- to 20-fold higher than in an aqueous medium, demonstrating the usefulness of double-phase systems for this particular biotransformation [6].
• Simultaneous induction tests with cells grown on styrene or toluene showed high rates of oxygen consumption with toluene cis-glycol and 3-methylcatechol, suggesting the involvement of a cis-glycol pathway [7].
• Ion-exchange chromatography yielded three protein fractions (A, B, and C) which were all required for the oxidation of 2NT to 3-methylcatechol and nitrite [8].

Chemical compound and disease context of 3-Methyl-1, 2-dihydroxybenzene

• Partially purified preparations of catechol 2,3-dioxygenase from toluene-grown cells of Pseudomonas putida catalyzed the stoichiometric oxidation of 3-methylcatechol to 2-hydroxy-6-oxohepta-2,4-dienoate [9].
• Pseudomonas species isolated from cattle dip tanks initially metabolized 2,4-dimethylaniline by oxidative deamination, following a degradation pathway via a 3-methylcatechol intermediate [10].
• Bioproduction of 3-methylcatechol from toluene by Pseudomonas putida MC2 was studied in the presence of an additional 1-octanol phase [11].

Biological context of 3-Methyl-1, 2-dihydroxybenzene

• The enzyme had a broad substrate specificity and catalyzed the oxidation of catechol, 4-methylcatechol, 3-methylcatechol, and 3-isopropyl catechol [12].
• The genes encoding enzymes for meta cleavage of catechol or 3-methylcatechol, derived from catabolism of these substrates, were subcloned from pRO1957 and were shown to be organized into a single operon with the promoter proximal to tbuE [13].
• The deduced amino acid sequence of catechol 2,3-dioxygenase from P. cepacia G4 exhibited 79-82% homologies with those of 3-methylcatechol 2,3-dioxygenase of P. putida UCC2 and catechol 2,3-dioxygenase of P. pickettii PKO1 [14].
• It is shown that a single amino acid substitution present in the NahH sequence, His250-->Gln, was responsible for the reduced kcat and increased kinact values for 3-methylcatechol [15].
• We also show that the binding site of 3-methylcatechol for suicide inhibition is different from the catalytic site [15].

Anatomical context of 3-Methyl-1, 2-dihydroxybenzene

• The cytotoxic effects for these BTEX metabolites to Hela cells were 3-methylcatechol > 4-methylcatechol > 4-hydroxy-3-methoxybenzoic acid > 4-hydroxybenzoic acid [16].

Associations of 3-Methyl-1, 2-dihydroxybenzene with other chemical compounds

• A straightforward stable isotope dilution analysis (SIDA) for the quantitative determination of the di- and trihydroxybenzenes catechol (1), pyrogallol (2), 3-methylcatechol (3), 4-methylcatechol (4), and 4-ethylcatechol (5) in foods by means of liquid chromatography-tandem mass spectrometry was developed [17].

Gene context of 3-Methyl-1, 2-dihydroxybenzene

• In cell extracts, 3-methylcatechol was degraded by both catechol 1,2- and catechol 2,3-dioxygenase [18].
• The NahH catechol 2,3-dioxygenase was partially deficient in oxidizing 3-methylcatechol due to defects in two catalytic properties [15].

References