IUBMB Enzyme Nomenclature

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, CAS registry number:

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. [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. [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. [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. [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. [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. [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. [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. [PMID: 31750652]

[EC 1.13.11.91 created 2020]


Return to EC 1.13.11 home page
Return to EC 1.13 home page
Return to EC 1 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page