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Literature summary for 1.13.11.85 extracted from

  • Seidel, J.; Schmitt, G.; Hoffmann, M.; Jendrossek, D.; Einsle, O.
    Structure of the processive rubber oxygenase RoxA from Xanthomonas sp (2013), Proc. Natl. Acad. Sci. USA, 110, 13833-13838 .
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method, structural analysis of RoxA from Xanthomonas sp. strain 35Y at a resolution of 1.8 A Xanthomonas sp. 35Y
to 1.8 A resolution. The enzyme shows an unusually low degree of secondary structure. RoxA incorporates both oxygen atoms of its cosubstrate dioxygen into the rubber cleavage product 12-oxo-4,8-dimethyl-trideca-4,8-diene-1-al Streptomyces sp. K30

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
rubber latex + O2 Xanthomonas sp. 35Y the enzyme is excreted by Xanthomonas to functionalize and cleave the inert latex biopolymer poly(cis-1,4-isoprene) into the more soluble (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal units (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
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 ?

Organism

Organism UniProt Comment Textmining
Streptomyces sp. K30 Q3L8N0
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Xanthomonas sp. 35Y Q7X0P3
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
rubber latex + O2 the enzyme is excreted by Xanthomonas to functionalize and cleave the inert latex biopolymer poly(cis-1,4-isoprene) into the more soluble (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal units Xanthomonas sp. 35Y (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
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 ?
rubber latex + O2 the enzyme incorporates both oxygen atoms of its cosubstrate dioxygen into the rubber cleavage product (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal. Activation and cleavage of O2 require binding of polyisoprene, and thus the substrate needs to use hydrophobic access channels to reach the deeply buried active site of RoxA. The location and nature of these channels support a processive mechanism of latex cleavage Xanthomonas sp. 35Y (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
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 ?

Synonyms

Synonyms Comment Organism
roxA
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 Xanthomonas sp. 35Y
rubber oxygenase A
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 Xanthomonas sp. 35Y

Cofactor

Cofactor Comment Organism Structure
heme a diheme c-type cytochrome Xanthomonas sp. 35Y

General Information

General Information Comment Organism
metabolism the enzyme is excreted by Xanthomonas to functionalize and cleave the inert latex biopolymer poly(cis-1,4-isoprene) into the more soluble (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal units Xanthomonas sp. 35Y
physiological function RoxA is isolated with O2 stably bound to the active site heme iron. Activation and cleavage of O2 require binding of polyisoprene, and the substrate needs to use hydrophobic access channels to reach the deeply buried active site of RoxA. Both residues H312 and Y462 are ideally positioned to form hydrogen bonds that arrest the substrate chain, so that the bond connecting the third and fourth monomer is in close proximity to the O2 ligand at heme 1. After oxidative cleavage, the resulting 2-oxo-4,8-dimethyl-trideca-4,8-diene-1-al product dissociates, and RoxA slides along the isoprene chain until the terminus is again arrested by hydrogen bonds Streptomyces sp. K30