EC
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1.5.99.1
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Transferred entry: | sarcosine dehydrogenase. Now EC 1.5.8.3, sarcosine dehydrogenase
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[EC 1.5.99.1 created 1972, deleted 2012] |
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EC
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1.5.99.10
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Transferred entry: | dimethylamine dehydrogenase. Now EC 1.5.8.1, dimethylamine dehydrogenase
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[EC 1.5.99.10 created 1999, deleted 2002] |
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EC
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1.5.99.11
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Transferred entry: | methylenetetrahydromethanopterin dehydrogenase. As the acceptor is known the enzyme has been transferred to EC 1.5.98.2, 5,10-methylenetetrahydromethanopterin reductase
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[EC 1.5.99.11 created 2000, modified 2004, deleted 2014] |
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EC |
1.5.99.12 |
Accepted name: |
cytokinin dehydrogenase |
Reaction: |
N6-prenyladenine + acceptor + H2O = adenine + 3-methylbut-2-enal + reduced acceptor |
Glossary: |
zeatin = (E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol = (E)-N6-(4-hydroxy-3-methylbut-2-enyl)adenine
N6-prenyladenine = N6-(3-methylbut-2-en-1-yl)purin-6-amine |
Other name(s): |
N6-dimethylallyladenine:(acceptor) oxidoreductase; 6-N-dimethylallyladenine:acceptor oxidoreductase; OsCKX2; CKX; cytokinin oxidase/dehydrogenase; N6-dimethylallyladenine:acceptor oxidoreductase |
Systematic name: |
N6-prenyladenine: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 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 copper(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] |
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[EC 1.5.99.12 created 2001] |
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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] |
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[EC 1.5.99.13 created 2010, modified 2011] |
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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 |
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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, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB |
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] |
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[EC 1.5.99.14 created 2012] |
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EC |
1.5.99.15 |
Accepted name: |
dihydromethanopterin reductase (acceptor) |
Reaction: |
5,6,7,8-tetrahydromethanopterin + oxidized acceptor = 7,8-dihydromethanopterin + reduced acceptor |
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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 folate analogue 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] |
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[EC 1.5.99.15 created 2014] |
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