The Enzyme Database

Your query returned 7 entries.    printer_iconPrintable version



EC 1.5.99.1      
Transferred entry: sarcosine dehydrogenase. Now EC 1.5.8.3, sarcosine dehydrogenase
[EC 1.5.99.1 created 1972, deleted 2012]
 
 
EC 1.5.99.10      
Transferred entry: dimethylamine dehydrogenase. Now EC 1.5.8.1, dimethylamine dehydrogenase
[EC 1.5.99.10 created 1999, deleted 2002]
 
 
EC 1.5.99.11      
Transferred entry: methylenetetrahydromethanopterin dehydrogenase. As the acceptor is known the enzyme has been transferred to EC 1.5.98.2, 5,10-methylenetetrahydromethanopterin reductase
[EC 1.5.99.11 created 2000, modified 2004, deleted 2014]
 
 
EC 1.5.99.12     
Accepted name: cytokinin dehydrogenase
Reaction: N6-dimethylallyladenine + acceptor + H2O = adenine + 3-methylbut-2-enal + reduced acceptor
For diagram of reaction, click here
Glossary: zeatin = (E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol = (E)-N6-(4-hydroxy-3-methylbut-2-enyl)adenine
Other name(s): N6-dimethylallyladenine:(acceptor) oxidoreductase; 6-N-dimethylallyladenine:acceptor oxidoreductase; OsCKX2; CKX; cytokinin oxidase/dehydrogenase
Systematic name: N6-dimethylallyladenine:acceptor oxidoreductase
Comments: A flavoprotein(FAD). Catalyses the oxidation of cytokinins, a family of N6-substituted adenine derivatives that are plant hormones, where the substituent is a dimethylallyl or other prenyl group. Although this activity was previously thought to be catalysed by a hydrogen-peroxide-forming oxidase, this enzyme does not require oxygen for activity and does not form hydrogen peroxide. 2,6-Dichloroindophenol, methylene blue, nitroblue tetrazolium, phenazine methosulfate and Cu(II) in the presence of imidazole can act as acceptors. This enzyme plays a part in regulating rice-grain production, with lower levels of the enzyme resulting in enhanced grain production [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 55326-39-1
References:
1.  Galuszka, P., Frebort, I., Sebela, M., Jacobsen, S. and Pec, P. Cytokinin oxidase or dehydrogenase? Mechanism of cytokinin degradation in plants. Eur. J. Biochem. 268 (2001) 450–461. [DOI] [PMID: 11168382]
2.  Ashikari, M., Sakakibara, H., Lin, S., Yamamoto, T., Takashi, T., Nishimura, A., Angeles, E.R., Qian, Q., Kitano, H. and Matsuoka, M. Cytokinin oxidase regulates rice grain production. Science 309 (2005) 741–745. [DOI] [PMID: 15976269]
[EC 1.5.99.12 created 2001]
 
 
EC 1.5.99.13     
Accepted name: D-proline dehydrogenase
Reaction: D-proline + acceptor = 1-pyrroline-2-carboxylate + reduced acceptor
Other name(s): D-Pro DH; D-Pro dehydrogenase; dye-linked D-proline dehydrogenase
Systematic name: D-proline:acceptor oxidoreductase
Comments: A flavoprotein (FAD). The enzyme prefers D-proline and acts on other D-amino acids with lower efficiency.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Tani, Y., Tanaka, K., Yabutani, T., Mishima, Y., Sakuraba, H., Ohshima, T. and Motonaka, J. Development of a D-amino acids electrochemical sensor based on immobilization of thermostable D-proline dehydrogenase within agar gel membrane. Anal. Chim. Acta 619 (2008) 215–220. [DOI] [PMID: 18558115]
2.  Satomura, T., Kawakami, R., Sakuraba, H. and Ohshima, T. Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase. J. Biol. Chem. 277 (2002) 12861–12867. [DOI] [PMID: 11823469]
[EC 1.5.99.13 created 2010, modified 2011]
 
 
EC 1.5.99.14     
Accepted name: 6-hydroxypseudooxynicotine dehydrogenase
Reaction: 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + acceptor + H2O = 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + reduced acceptor
For diagram of nicotine catabolism by arthrobacter, click here
Glossary: 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 6-hydroxypseudooxynicotine
1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 2,6-dihydroxypseudooxynicotine
Systematic name: 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one:acceptor 6-oxidoreductase (hydroxylating)
Comments: Contains a cytidylyl molybdenum cofactor [3]. The enzyme, which participates in the nicotine degradation pathway, has been characterized from the soil bacterium Arthrobacter nicotinovorans [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD
References:
1.  Freudenberg, W., Konig, K. and Andreesen, J. R. Nicotine dehydrogenase from Arthrobacter oxidans: A molybdenum-containing hydroxylase. FEMS Microbiology Letters 52 (1988) 13–18.
2.  Grether-Beck, S., Igloi, G.L., Pust, S., Schilz, E., Decker, K. and Brandsch, R. Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans. Mol. Microbiol. 13 (1994) 929–936. [DOI] [PMID: 7815950]
3.  Sachelaru, P., Schiltz, E. and Brandsch, R. A functional mobA gene for molybdopterin cytosine dinucleotide cofactor biosynthesis is required for activity and holoenzyme assembly of the heterotrimeric nicotine dehydrogenases of Arthrobacter nicotinovorans. Appl. Environ. Microbiol. 72 (2006) 5126–5131. [DOI] [PMID: 16820521]
[EC 1.5.99.14 created 2012]
 
 
EC 1.5.99.15     
Accepted name: dihydromethanopterin reductase (acceptor)
Reaction: 5,6,7,8-tetrahydromethanopterin + oxidized acceptor = 7,8-dihydromethanopterin + reduced acceptor
For diagram of methanopterin biosynthesis (part 4), click here
Other name(s): DmrX
Systematic name: 5,6,7,8-tetrahydromethanopterin:acceptor 5,6-oxidoreductase
Comments: This archaeal enzyme catalyses the last step in the biosynthesis of tetrahydromethanopterin, a coenzyme used in methanogenesis. The enzyme, characterized from the archaea Methanosarcina mazei and Methanocaldococcus jannaschii, is an iron-sulfur flavoprotein. cf. EC 1.5.1.47, dihydromethanopterin reductase [NAD(P)+].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wang, S., Tiongson, J. and Rasche, M.E. Discovery and characterization of the first archaeal dihydromethanopterin reductase, an iron-sulfur flavoprotein from Methanosarcina mazei. J. Bacteriol. 196 (2014) 203–209. [DOI] [PMID: 23995635]
[EC 1.5.99.15 created 2014]
 
 


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