Entry
Name
exo-cleaving rubber dioxygenase;
roxA (gene name);
heme-dependent rubber oxygenase (ambiguous)
Class
Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of two atoms of oxygen
BRITE hierarchy
Sysname
cis-1,4-polyisoprene:oxygen dioxygenase [(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal-forming]
Reaction(IUBMB)
cis-1,4-polyisoprene + n O2 = n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal [RN:
R11999 ]
Reaction(KEGG)
Substrate
Product
(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal [CPD:
C21834 ]
Comment
The enzyme, studied mainly from the bacterium Xanthomonas sp. 35Y, catalyses the cleavage of the double bonds in natural and synthetic rubber (cis-1,4-polyisoprene polymers), generating ends that contain ketone and aldehyde groups. The enzyme from Xanthomonas sp. 35Y contains two c-type cytochromes. It attacks the substrate from its end, producing a single product of 15 carbons.
History
EC 1.13.11.85 created 2018
Orthology
K22690 exo-cleaving rubber dioxygenase
Genes
» show all
Taxonomy
Reference
Authors
Tsuchii A, Takeda K
Title
Rubber-degrading enzyme from a bacterial culture.
Journal
Reference
Authors
Jendrossek D, Reinhardt S
Title
Sequence analysis of a gene product synthesized by Xanthomonas sp. during growth on natural rubber latex.
Journal
Reference
Authors
Braaz R, Fischer P, Jendrossek D
Title
Novel type of heme-dependent oxygenase catalyzes oxidative cleavage of rubber (poly-cis-1,4-isoprene).
Journal
Reference
Authors
Braaz R, Armbruster W, Jendrossek D
Title
Heme-dependent rubber oxygenase RoxA of Xanthomonas sp. cleaves the carbon backbone of poly(cis-1,4-Isoprene) by a dioxygenase mechanism.
Journal
Sequence
Reference
Authors
Seidel J, Schmitt G, Hoffmann M, Jendrossek D, Einsle O
Title
Structure of the processive rubber oxygenase RoxA from Xanthomonas sp.
Journal
Sequence
Reference
Authors
Birke J, Jendrossek D
Title
Rubber oxygenase and latex clearing protein cleave rubber to different products and use different cleavage mechanisms.
Journal
Other DBs