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Literature summary extracted from

  • Beller, H.; Rodrigues, A.; Zargar, K.; Wu, Y.; Saini, A.; Saville, R.; Pereira, J.; Adams, P.; Tringe, S.; Petzold, C.; Keasling, J.
    Discovery of enzymes for toluene synthesis from anoxic microbial communities (2018), Nat. Chem. Biol., 14, 451-457 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.119 poor solubility of the recombinant protein when expressed in Escherichia coli uncultured bacterium

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.119 molecular modeling of the substrate-bound active sites of PhdB. Important conserved residues, are the sites of the thiyl radical, Cys482 and glycyl radical ,Gly815. PhdB has a hydrophobic pocket including Trp495, Tyr691, and Val693 accommodating the unsubstituted ring of phenylacetate uncultured bacterium

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.119 G815A mutation of the putative site of the glycyl radical, loss of activity uncultured bacterium

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.119 uncultured bacterium A0A2P1UAH5
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.119 additional information glycyl radical enzyme. Poor substrate: 4-hydroxyphenylacetate uncultured bacterium ?
-
 ?
4.1.1.119 phenylacetate
-
 uncultured bacterium toluene + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.119 phdB
-
 uncultured bacterium

General Information

EC Number General Information Comment Organism
4.1.1.119 physiological function toluene-producing enzyme PhdB is a glycyl radical enzyme of bacterial origin that catalyzes phenylacetate decarboxylation. Its cognate activating enzyme is PhdA, a radical S-adenosylmethionine enzyme, discovered in two distinct anoxic microbial communities that produce toluene uncultured bacterium