EC Number |
General Information |
Reference |
---|
1.13.11.85 | malfunction |
Gram-negative rubber-degrading bacteria generally utilise two synergistically acting rubber oxygenases (RoxA/RoxB) for efficient cleavage of polyisoprene to (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal |
-, 746860 |
1.13.11.85 | metabolism |
the enzyme is essential for the poly(cis-1,4-isoprene) rubber utilization of its host strain |
-, 764327 |
1.13.11.85 | 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 |
746289 |
1.13.11.85 | physiological function |
expression of gene functionally complements a Xanthomonas sp. 35Y RoxA deletion mutant |
744094 |
1.13.11.85 | physiological function |
inactivation of the chromosomal roxA gene results in inability of Xanthomonas sp. to produce active RoxA and to utilize rubber as a sole source of carbon and energy |
745192 |
1.13.11.85 | 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 |
746289 |