3,4-dihydroxybenzoate decarboxylase in Enterobacter cloacae P241 is induced by adding 3,4-dihydroxybenzoic acid, 3-hydroxybenzoic acid, 3,4,5-trihydroxybenzoic acid or 4-acetamidobenzoic acid to the culture medium

2 entries

Enterobacter cloacae

714574

Enterobacter cloacae P241

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UNIPROT

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LITERATURE

synthesis

4 entries

synthesis

Enterobacter cloacae subsp. cloacae

A0A0H3CJN8

engineering of Pseudomonas putida KT2440 to produce muconate from either aromatic molecules or sugars. Coexpression of protocatechuate decarboxylase and associated proteins reduces protocatechuate accumulation and enhances muconate production relative to strains expressing the protocatechuate decarboxylase alone. In bioreactor experiments, coexpression increases the specific productivity of muconate from the lignin monomer p-coumarate by 50% and results in a titer of >15 g/l. In strains engineered to produce muconate from glucose, coexpression more than triples the titer, yield, productivity, and specific productivity, with the best strain producing 4.92Â±0.48 g/l muconate

748563

synthesis

Klebsiella pneumoniae subsp. pneumoniae

B9A9M6

increase in protocatechuate decarboxylase activity in Escherichia coli through enhanced expression of both protocatechuate decarboxylase AroYand kpdB encoding the B-subunit of 4-hydroxybenzoate decarboxylase. This permits expression of protocatechuate decarboxylase activity at a level approximately 14fold greater than the strain with aroY only. The expression level of AroY increases, apparently as a function of the coexpression of AroY and KpdB

748264

synthesis

Enterobacter cloacae

production of the 4-hydroxybenzoate, protocatechuate, and catechol in Escherichia coli. To enhance endogenous biosynthesis of 4-hydroxybenzoate, native chorismate pyruvate lyase ubiC is overexpressed. 4-Hydroxybenzoate is converted to protocatechuate by hydroxylase pobA from Pseudomonas aeruginosa. Catechol is produced by the additional coexpression of protocatechuate decarboxylase from Enterobacter cloacae. Systematic expression of appropriate pathway elements in phenylalanine overproducing Escherichia coli enables initial titers of 32, 110, and 81 mg/l for 4-hydroxybenzoate, protocatechuate, and catechol, respectively. Disruption of chorismate mutase/prephenate dehydratase (pheA) to preserve endogenous chorismate then allows maximum titers of 277, 454, and 451 mg/l, respectively, at glucose yields of 5.8, 9.7, and 14.3% of their respective theoretical maxima

749197

synthesis

Enterobacter cloacae subsp. cloacae DSM 30054

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AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

4728

Grant, D.J.W.; Patel, J.C.

The non-oxidative decarboxylation of p-hydroxybenzoic acid, gentisic acid, protocatechuic acid and gallic acid by Klebsiella aerogenes (Aerobacter aerogenes)

Antonie van Leeuwenhoek

325-343

1969

Klebsiella aerogenes, Rhodopseudomonas sp.

5309907

brenda

4747

He, Z.; Wiegel, J.

Purification and characterization of an oxygen-sensitive reversible 3,4-dihydroxybenzoate decarboxylase from Clostridium hydroxybenzoicum

J. Bacteriol.

178

3539-3543