The Enzyme Database

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EC 1.13.11.91     
Accepted name: 3-mercaptopropionate dioxygenase
Reaction: 3-sulfanylpropanoate + O2 = 3-sulfinopropanoate
Other name(s): mdo (gene name); 3-mercaptopropionic acid dioxygenase; 3-sulfanylpropanoate dioxygenase
Systematic name: 3-sulfanylpropanoate:oxygen oxidoreductase
Comments: This bacterial enzyme contains an iron(2+) atom coordinated by three protein-derived histidines and a Ser-His-Tyr motif. It is similar to EC 1.13.11.20, cysteine dioxygenase, and can act on L-cysteine, but has a much higher activity with its native substrate, 3-sulfanylpropanoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bruland, N., Wubbeler, J.H. and Steinbuchel, A. 3-Mercaptopropionate dioxygenase, a cysteine dioxygenase homologue, catalyzes the initial step of 3-mercaptopropionate catabolism in the 3,3-thiodipropionic acid-degrading bacterium Variovorax paradoxus. J. Biol. Chem. 284 (2009) 660–672. [DOI] [PMID: 19001372]
2.  Driggers, C.M., Hartman, S.J. and Karplus, P.A. Structures of Arg- and Gln-type bacterial cysteine dioxygenase homologs. Protein Sci. 24 (2015) 154–161. [DOI] [PMID: 25307852]
3.  Pierce, B.S., Subedi, B.P., Sardar, S. and Crowell, J.K. The ’Gln-type’ thiol dioxygenase from Azotobacter vinelandii is a 3-mercaptopropionic acid dioxygenase. Biochemistry 54 (2015) 7477–7490. [DOI] [PMID: 26624219]
4.  Tchesnokov, E.P., Fellner, M., Siakkou, E., Kleffmann, T., Martin, L.W., Aloi, S., Lamont, I.L., Wilbanks, S.M. and Jameson, G.N. The cysteine dioxygenase homologue from Pseudomonas aeruginosa is a 3-mercaptopropionate dioxygenase. J. Biol. Chem. 290 (2015) 24424–24437. [DOI] [PMID: 26272617]
5.  Fellner, M., Aloi, S., Tchesnokov, E.P., Wilbanks, S.M. and Jameson, G.N. Substrate and pH-dependent kinetic profile of 3-mercaptopropionate dioxygenase from Pseudomonas aeruginosa. Biochemistry 55 (2016) 1362–1371. [DOI] [PMID: 26878277]
6.  Crowell, J.K., Sardar, S., Hossain, M.S., Foss, F.W., Jr. and Pierce, B.S. Non-chemical proton-dependent steps prior to O2-activation limit Azotobacter vinelandii 3-mercaptopropionic acid dioxygenase (MDO) catalysis. Arch. Biochem. Biophys. 604 (2016) 86–94. [DOI] [PMID: 27311613]
7.  Aloi, S., Davies, C.G., Karplus, P.A., Wilbanks, S.M. and Jameson, G.NL. Substrate specificity in thiol dioxygenases. Biochemistry 58 (2019) 2398–2407. [DOI] [PMID: 31045343]
8.  Sardar, S., Weitz, A., Hendrich, M.P. and Pierce, B.S. Outer-sphere tyrosine 159 within the 3-mercaptopropionic acid dioxygenase S-H-Y motif gates substrate-coordination denticity at the non-heme iron active site. Biochemistry 58 (2019) 5135–5150. [DOI] [PMID: 31750652]
[EC 1.13.11.91 created 2020]
 
 


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