IUBMB Enzyme Nomenclature

EC 3.1.3.104

Accepted name: 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase

Reaction: 5-amino-6-(5-phospho-D-ribitylamino)uracil + H2O = 5-amino-6-(D-ribitylamino)uracil + phosphate

Other name(s): 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate phosphatase

Systematic name: 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphohydrolase

Comments: Requires Mg2+. The enzyme, which is found in plants and bacteria, is part of a pathway for riboflavin biosynthesis. Most forms of the enzyme has a broad substrate specificity [1,3].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Haase, I., Sarge, S., Illarionov, B., Laudert, D., Hohmann, H.P., Bacher, A. and Fischer, M. Enzymes from the haloacid dehalogenase (HAD) superfamily catalyse the elusive dephosphorylation step of riboflavin biosynthesis. Chembiochem 14 (2013) 2272-2275. [PMID: 24123841]

2. London, N., Farelli, J.D., Brown, S.D., Liu, C., Huang, H., Korczynska, M., Al-Obaidi, N.F., Babbitt, P.C., Almo, S.C., Allen, K.N. and Shoichet, B.K. Covalent docking predicts substrates for haloalkanoate dehalogenase superfamily phosphatases. Biochemistry 54 (2015) 528-537. [PMID: 25513739]

3. Sarge, S., Haase, I., Illarionov, B., Laudert, D., Hohmann, H.P., Bacher, A. and Fischer, M. Catalysis of an essential step in vitamin B2 biosynthesis by a consortium of broad spectrum hydrolases. ChemBioChem 16 (2015) 2466-2469. [PMID: 26316208]

[EC 3.1.3.104 created 2016]


Return to EC 3.1.3 home page
Return to EC 3.1 home page
Return to EC 3 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page