Reference on EC 3.13.1.4 - 3-sulfinopropanoyl-CoA desulfinase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wuebbeler, J.H.; Bruland, N.; Kretschmer, K.; Steinbuechel, A.
Novel pathway for catabolism of the organic sulfur compound 3,3-dithiodipropionic acid via 3-mercaptopropionic acid and 3-Sulfinopropionic acid to propionyl-coenzyme A by the aerobic bacterium Tetrathiobacter mimigardefordensis strain DPN7
Appl. Environ. Microbiol.
74
4028-4035
2008
Advenella mimigardefordensis, Advenella mimigardefordensis DPN7
Schürmann, M.; Deters, A.; Wübbeler, J.H.; Steinbüchel, A.
A novel 3-sulfinopropionyl coenzyme A (3SP-CoA) desulfinase from Advenella mimigardefordensis strain DPN7T acting as a key enzyme during catabolism of 3,3'-dithiodipropionic acid is a member of the acyl-CoA dehydrogenase superfamily
J. Bacteriol.
195
1538-1551
2013
Advenella mimigardefordensis, Advenella mimigardefordensis DPN7T
Schürmann, M.; Demming, R.M.; Krewing, M,; Rose, J.; Wübbeler, J.H.; Steinbüchel A.
Identification of 3-sulfinopropionyl coenzyme A (CoA) desulfinases within the acyl-CoA dehydrogenase superfamily
J. Bacteriol.
196
882-893
2014
Cupriavidus necator, Variovorax paradoxus, Paraburkholderia xenovorans, Advenella mimigardefordensis, Advenella mimigardefordensis DPN7, Cupriavidus necator N-1, Variovorax paradoxus TBEA6
Schuermann, M.; Meijers, R.; Schneider, T.R.; Steinbuechel, A.; Cianci, M.
3-Sulfinopropionyl-coenzyme A (3SP-CoA) desulfinase from Advenella mimigardefordensis DPN7(T): crystal structure and function of a desulfinase with an acyl-CoA dehydrogenase fold
Acta Crystallogr. Sect. D
71
1360-1372
2015
Advenella mimigardefordensis (K4L7X3), Advenella mimigardefordensis, Advenella mimigardefordensis DPN7T (K4L7X3)
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