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Literature summary for 1.14.13.33 extracted from

  • Kuatsjah, E.; Johnson, C.; Salvachua, D.; Werner, A.; Zahn, M.; Szostkiewicz, C.; Singer, C.; Dominick, G.; Okekeogbu, I.; Haugen, S.; Woodworth, S.; Ramirez, K.; Giannone, R.; Hettich, R.; McGeehan, J.; Beckham, G.
    Debottlenecking 4-hydroxybenzoate hydroxylation in Pseudomonas putida KT2440 improves muconate productivity from p-coumarate (2022), Metab. Eng., 70, 31-42 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene praI, functional recombinant expression in different strains of Pseudomonas putida replacing the endogenous gene pobA that encodes a PHBH enzyme Paenibacillus sp. JJ-1b

Protein Variants

Protein Variants Comment Organism
additional information in Pseudomonas putida KT2440 strains engineered to convert lignin-related aromatic compounds to muconic acid (MA), PHBH activity is rate-limiting, as indicated by the accumulation of 4-HBA, which ultimately limits MA productivity. Replacement of PobA, the native Pseudomonas putida PHBH, with PraI, a PHBH from Paenibacillus sp. JJ-1b with a broader nicotinamide cofactor preference, can alleviate this bottleneck Paenibacillus sp. JJ-1b
additional information in Pseudomonas putida KT2440 strains engineered to convert lignin-related aromatic compounds to muconic acid (MA), PHBH activity is rate-limiting, as indicated by the accumulation of 4-hydroxybenzoate (4-HBA), which ultimately limits MA productivity. Replacement of PobA, the native Pseudomonas putida PHBH, with PraI, a PHBH from Paenibacillus sp. JJ-1b with a broader nicotinamide cofactor preference, can alleviate this bottleneck. Comparison of three Pseudomonas putida strains engineered to produce MA from p-coumarate (pCA), showing that expression of praI leads to lower 4-HBA accumulation and decreased NADP+/NADPH ratios relative to strains harboring pobA, indicative of a relieved 4-HBA bottleneck due to increased NADPH availability. In bioreactor cultivations, a strain exclusively expressing praI achieved a titer of 40 g/l MA at 100% molar yield and a productivity of 0.5 g/l/h Pseudomonas putida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-hydroxybenzoate + NADH + H+ + O2 Pseudomonas putida
-
3,4-dihydroxybenzoate + NAD+ + H2O
-
?
4-hydroxybenzoate + NADH + H+ + O2 Paenibacillus sp. JJ-1b
-
3,4-dihydroxybenzoate + NAD+ + H2O
-
?
4-hydroxybenzoate + NADPH + H+ + O2 Pseudomonas putida
-
3,4-dihydroxybenzoate + NADP+ + H2O
-
?
4-hydroxybenzoate + NADPH + H+ + O2 Paenibacillus sp. JJ-1b
-
3,4-dihydroxybenzoate + NADP+ + H2O
-
?

Organism

Organism UniProt Comment Textmining
Paenibacillus sp. JJ-1b C4TP09
-
-
Pseudomonas putida Q9R9T1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxybenzoate + NADH + H+ + O2
-
Pseudomonas putida 3,4-dihydroxybenzoate + NAD+ + H2O
-
?
4-hydroxybenzoate + NADH + H+ + O2
-
Paenibacillus sp. JJ-1b 3,4-dihydroxybenzoate + NAD+ + H2O
-
?
4-hydroxybenzoate + NADPH + H+ + O2
-
Pseudomonas putida 3,4-dihydroxybenzoate + NADP+ + H2O
-
?
4-hydroxybenzoate + NADPH + H+ + O2
-
Paenibacillus sp. JJ-1b 3,4-dihydroxybenzoate + NADP+ + H2O
-
?

Synonyms

Synonyms Comment Organism
para-hydroxybenzoate-3-hydroxylases
-
Pseudomonas putida
para-hydroxybenzoate-3-hydroxylases
-
Paenibacillus sp. JJ-1b
PHBH
-
Pseudomonas putida
PHBH
-
Paenibacillus sp. JJ-1b
PobA
-
Pseudomonas putida
PRAI
-
Paenibacillus sp. JJ-1b

Cofactor

Cofactor Comment Organism Structure
additional information enzyme PraI can use NADPH and also efficiently utilizes NADH at roughly half the catalytic efficiency Paenibacillus sp. JJ-1b
additional information strict preference of NADPH for PobA Pseudomonas putida
NADH
-
Paenibacillus sp. JJ-1b
NADPH
-
Pseudomonas putida
NADPH
-
Paenibacillus sp. JJ-1b

General Information

General Information Comment Organism
additional information the X-ray crystal structure of PraI is solved and reveals absolute conservation of the active site architecture to other PHBH structures despite their differing cofactor preferences Paenibacillus sp. JJ-1b
physiological function the transformation of 4-hydroxybenzoate (4-HBA) to protocatechuate (PCA) is catalyzed by flavoprotein oxygenases known as para-hydroxybenzoate-3-hydroxylases (PHBHs) Pseudomonas putida
physiological function the transformation of 4-hydroxybenzoate (4-HBA) to protocatechuate (PCA) is catalyzed by flavoprotein oxygenases known as para-hydroxybenzoate-3-hydroxylases (PHBHs) Paenibacillus sp. JJ-1b