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Literature summary extracted from

  • Miao, L.; Li, Q.; Diao, A.; Zhang, X.; Ma, Y.
    Construction of a novel phenol synthetic pathway in Escherichia coli through 4-hydroxybenzoate decarboxylation (2015), Appl. Microbiol. Biotechnol., 99, 5163-5173 .
    View publication on PubMed

Application

EC Number Application Comment Organism
4.1.1.61 synthesis construction of a phenol synthetic pathway in Escherichia coli via overexpression of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase and chorismate pyruvate lyase. Phenol titer increases 147-fold after modulating the 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, chorismate pyruvate lyase, and 4-hydroxybenzoate decarboxylase genes in the chromosome. Tributyrin and dibutyl phthalate are the best two solvents for improving phenol production Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.1.99.2 S51A site-directed mutagenesis, the mutation leads to a decrease of the kcat/Km parameter for reactions with L-tyrosine and 3-fluoro-L-tyrosine by three orders of magnitude, compared to the wild-type enzyme, phenotype, overview. Influence of replacement of Ser51 by Ala on the kinetic parameters of TPL reactions with inhibitory L-phenylalanine and L-methionine, kinetics and structures, overview Citrobacter freundii

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.99.2 L-methionine inhibition of alpha,beta-elimination reaction Citrobacter freundii
4.1.99.2 L-phenylalanine inhibition of alpha,beta-elimination reaction Citrobacter freundii
4.1.99.2 additional information The mutant S51A also shows intermediate formation with L-Met and L-Phe. Influence of replacement of Ser51 by Ala on the kinetic parameters of TPL reactions with L-phenylalanine and L-methionine, kinetics and structures, overview Citrobacter freundii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.99.2 additional information
-
 additional information steady-state kinetics Citrobacter freundii
4.1.99.2 0.1
-
 3-fluoro-L-tyrosine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.12
-
 S-Benzyl-L-cysteine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.2
-
 L-tyrosine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.21
-
 S-(2-nitrophenyl)-L-cysteine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.8
-
 beta-chloro-L-alanine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 1.3
-
 L-tyrosine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 1.3
-
 3-fluoro-L-tyrosine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 1.57
-
 S-ethyl-L-cysteine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 2.12
-
 beta-chloro-L-alanine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 2.2
-
 S-(2-nitrophenyl)-L-cysteine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 2.32
-
 S-methyl-L-cysteine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 4.1
-
 S-Benzyl-L-cysteine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 5.4
-
 S-ethyl-L-cysteine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 10.5
-
 S-methyl-L-cysteine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.2 L-tyrosine + H2O Citrobacter freundii
-
 phenol + pyruvate + NH3
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.61 Escherichia coli AFH12530 and AFH12529 and AFH12528 AFH12530 i.e. subunit YclB, AFH12529 i.e. subunit YclC, AFH12528 i.e. subunit YclD
-
4.1.1.61 Escherichia coli ATCC 9637 AFH12530 and AFH12529 and AFH12528 AFH12530 i.e. subunit YclB, AFH12529 i.e. subunit YclC, AFH12528 i.e. subunit YclD
-
4.1.99.2 Citrobacter freundii P31013
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.99.2 L-tyrosine + H2O = phenol + pyruvate + NH3 mechanism of alpha,beta-elimination of L-tyrosine catalyzed by enzyme TPL Citrobacter freundii
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.2 3-fluoro-L-tyrosine + H2O
-
 Citrobacter freundii 3-fluorophenol + pyruvate + NH3
-
 r
4.1.99.2 beta-chloro-L-alanine + H2O
-
 Citrobacter freundii Cl- + pyruvate + NH3
-
 r
4.1.99.2 L-tyrosine + H2O
-
 Citrobacter freundii phenol + pyruvate + NH3
-
 r
4.1.99.2 additional information fragment of active site structure of the quinonoid complex of wild-type enzyme TPL with L-alanine, overview Citrobacter freundii ?
-
 ?
4.1.99.2 S-(2-nitrophenyl)-L-cysteine + H2O
-
 Citrobacter freundii 2-nitrobenzenethiolate + pyruvate + NH3
-
 r
4.1.99.2 S-benzyl-L-cysteine + H2O
-
 Citrobacter freundii thiophenol + pyruvate + NH3
-
 r
4.1.99.2 S-ethyl-L-cysteine + H2O
-
 Citrobacter freundii ethanethiol + pyruvate + NH3
-
 r
4.1.99.2 S-methyl-L-cysteine + H2O
-
 Citrobacter freundii methanethiol + pyruvate + NH3
-
 r

Synonyms

EC Number Synonyms Comment Organism
4.1.99.2 TPL
-
 Citrobacter freundii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.99.2 30
-
 assay at Citrobacter freundii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.99.2 0.012
-
 3-fluoro-L-tyrosine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.015
-
 S-Benzyl-L-cysteine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.03
-
 L-tyrosine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.044
-
 S-methyl-L-cysteine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.083
-
 S-ethyl-L-cysteine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.15
-
 beta-chloro-L-alanine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.63
-
 S-Benzyl-L-cysteine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 1.13
-
 S-methyl-L-cysteine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 1.4
-
 3-fluoro-L-tyrosine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 3.5
-
 L-tyrosine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 5.4
-
 S-ethyl-L-cysteine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 6
-
 beta-chloro-L-alanine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 8.7
-
 S-(2-nitrophenyl)-L-cysteine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 9.65
-
 S-(2-nitrophenyl)-L-cysteine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.99.2 8
-
 assay at Citrobacter freundii

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.2 pyridoxal 5'-phosphate dependent on Citrobacter freundii

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.1.99.2 additional information
-
 additional information rapid scanning stopped-flow kinetic experiments, kinetics Citrobacter freundii

General Information

EC Number General Information Comment Organism
4.1.99.2 additional information the Ser51 residue interacts with the side chain amino group of Lys257 at the stage of C-alpha-proton abstraction. This interaction ensures the correct orientation of the side chain of Lys257 accepting the C-alpha-proton of the external aldimine and stabilizes its ammonium form. Ser51 takes part in formation of a chain of hydrogen bonds which is necessary to perform the transfer of the Calpha-proton to the C-4'-position of the leaving phenol group in the reaction with the natural substrate. Ser51 is necessary for efficient C-alpha-proton abstraction and its following transfer to the 4'-position of the leaving phenol group in the alpha,beta-elimination reaction of L-tyrosine Citrobacter freundii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.99.2 0.0037
-
 S-Benzyl-L-cysteine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.0042
-
 S-methyl-L-cysteine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.0092
-
 3-fluoro-L-tyrosine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.015
-
 S-ethyl-L-cysteine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.022
-
 L-tyrosine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.19
-
 beta-chloro-L-alanine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 0.49
-
 S-methyl-L-cysteine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 2.84
-
 beta-chloro-L-alanine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 3.43
-
 S-ethyl-L-cysteine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 3.9
-
 S-(2-nitrophenyl)-L-cysteine recombinant mutant S51A, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 5.26
-
 S-Benzyl-L-cysteine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 14
-
 3-fluoro-L-tyrosine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 17.5
-
 L-tyrosine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii
4.1.99.2 46
-
 S-(2-nitrophenyl)-L-cysteine recombinant wild-type enzyme, pH 8.0, 30°C Citrobacter freundii