Literature summary for 4.1.1.119 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 .

Search for more literature for 4.1.1.119

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Organism

Organism	UniProt	Comment	Textmining
uncultured bacterium	A0A2P1UAH5	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
phdB	-	uncultured bacterium

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)