Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-methylpropane-1,2-diol + electron acceptor = 2-hydroxy-2-methylpropanal + reduced electron acceptor
-
D-fructose + electron acceptor = 5-dehydro-D-fructose + reduced electron acceptor
-
D-fructose + oxidized electron acceptor = 5-dehydro-D-fructose + reduced electron acceptor
-
H2 + electron acceptor = H+ + reduced electron acceptor
-
H2 + oxidized electron acceptor = H+ + reduced electron acceptor
-
2,6-dihydroxypyridine + NADH + electron acceptor = 2,3,6-trihydroxypyridine + NAD+ + reduced electron acceptor
-
NADH + electron acceptor + H2O = NAD+ + reduced electron acceptor
644584, 644587, 644581, 644590, 644568, 644574, 644580, 644579, 644583, 644604, 644578, 644598
-
NADPH + electron acceptor + H2O = NADP+ + reduced electron acceptor
-
nicotinate + H2O + electron acceptor = 6-hydroxynicotinate + reduced electron acceptor
-
CO + H2O + electron acceptor = CO2 + reduced electron acceptor
-
acetaldehyde + H2O + electron acceptor = acetate + reduced electron acceptor
-
benzaldehyde + H2O + electron acceptor = benzoate + reduced electron acceptor
-
L-thyroxine + electron acceptor = 3,3',5-triiodothyronine + iodide + reduced electron acceptor
-
diethylmethylamine + H2O + electron acceptor = diethylamine + formaldehyde + reduced electron acceptor
-
trimethylamine + H2O + electron acceptor = dimethylamine + formaldehyde + reduced electron acceptor
0, 393913, 393914, 393916, 393917, 393918, 393919, 393921, 393925, 393881, 393923, 393920
-
cis-zeatin + electron acceptor = (2Z)-4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
kinetin + electron acceptor = 2-furaldehyde + adenine + reduced electron acceptor
-
N-benzyladenine + electron acceptor = benzaldehyde + adenine + reduced electron acceptor
-
N6-(2-isopentenyl)adenine + electron acceptor = adenine + 3-methylbut-2-enal + reduced electron acceptor
-
N6-hexyladenine + electron acceptor = hexanal + adenine + reduced electron acceptor
-
N6-isopentenyl-2-(2-hydroxyethylamino)-9-methyladenine + electron acceptor = 3-methyl-2-butenal + 2-hydroxyethylamino-9-methyladenine + reduced electron acceptor
-
N6-isopentenyl-2-methylthioadenine + electron acceptor = 3-methyl-2-butenal + 2-methylthioadenine + reduced electron acceptor
-
N6-isopentenyladenine + CuCl2 = adenine + 3-methyl-2-butenal + reduced electron acceptor
-
N6-isopentenyladenine + electron acceptor = adenine + 3-methyl-2-butenal + reduced electron acceptor
288537, 288539, 288541, 288534, 288540, 0, 288542, 288535, 288536, 288544, 288543, 288533, 288538
-
N6-isopentenyladenosine + electron acceptor = 3-methylbut-2-enal + adenosine + reduced electron acceptor
-
trans-zeatin + electron acceptor = (2E)-4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
zeatin + electron acceptor = 4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
3,3'-diaminodipropylamine + electron acceptor = ? + reduced electron acceptor
-
monoacetylspermidine + electron acceptor = ? + reduced electron acceptor
-
N,N'-bis(3-aminopropyl)-1,3-propanediamine + electron acceptor = ? + reduced electron acceptor
-
N,N'-di(aminopropyl)-propanediamine + electron acceptor = ? + reduced electron acceptor
-
N-(3-aminopropyl)-1,3-diaminopropane + electron acceptor = ? + reduced electron acceptor
-
N-(3-aminopropyl)-1,3-propanediamine + electron acceptor = ? + reduced electron acceptor
-
N-(3-hydroxypropyl)-1,4-diaminobutane + electron acceptor = ? + reduced electron acceptor
-
N-alkylputrescine + electron acceptor = ? + reduced electron acceptor
-
N8-acetylspermidine + electron acceptor = ? + reduced electron acceptor
-
spermidine + electron acceptor = 1,3-diaminopropane + DELTA1-pyrroline + reduced electron acceptor
-
spermine + electron acceptor = ? + reduced electron acceptor
-
dimethylallyl diphosphate + all-trans-lycopene + acceptor + H2O = nonaflavuxanthin + reduced electron acceptor + diphosphate
-
dimethylallyl diphosphate + nonaflavuxanthin + acceptor + H2O = flavuxanthin + reduced electron acceptor + diphosphate
-
ADP + phosphate + 15,173-seco-F430-173-acid + electron acceptor = ATP + Ni-sirohydrochlorin a,c-diamide + reduced electron acceptor + H2O
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cytokinin oxidase or dehydrogenase? Mechanism of cytokinin degradation in cereals
2001
Galuszka, P.; Frebort, I.; Sebela, M.; Sauer, P.; Jacobsen, S.; Pec, P.
Eur. J. Biochem.
268
450-461
-
The purification of cytokinin oxidase from Zea mays kernels
1989
Burch, L.R.; Horgan, R.
Phytochemistry
28
1313-1319
-
Cytokinin catabolism and cytokinin oxidase
1983
McGaw, B.A.; Horgan, R.
Phytochemistry
22
1103-1105
Changes in cytokinin content and cytokinin oxidase activity in response to derepression of ipt gene transcription in transgenic tobacco calli and plants
1996
Motyka, V.; Faiss, M.; Strnad, M.; Kaminek, M.; Schmuelling, T.
Plant Physiol.
112
1035-1043
Cytokinin oxidase from Phaseolus vulgaris callus tissues. Enhanced in vitro activity of the enzyme in the presence of copper-imidazole complexes
1987
Chatfield, J.M.; Armstrong, D.J.
Plant Physiol.
84
726-731
Molecular and biochemical characterization of a cytokinin oxidase from maize
2001
Bilyeu, K.D.; Cole, J.L.; Laskey, J.G.; Riekhof, W.R.; Esparza, T.J.; Kramer, M.D.; Morris, R.O.
Plant Physiol.
125
378-386
Regulation of cytokinin oxidase activity in callus tissues of Phaseolus vulgaris L. cv Great Northern
1986
Chatfield, J.M.; Armstrong, D.J.
Plant Physiol.
80
493-499
-
Degradation of cytokinins by cytokinin oxidases in plants
2000
Galuszka, P.; Frebort, I.; Sebela, M.; Pec, P.
Plant Growth Regul.
32
315-327
-
Cytokinin oxidase: biochemical features and physiological significance
1994
Hare, P.D.; van Staden, J.
Physiol. Plant.
91
128-136
-
Changes in cytokinins and cytokinin oxidase activity in developing maize kernels and the effects of exogenous cytokinin on kernel development
1995
Dietrich, J.T.; Kaminek, M.; Blevins, D.G.; Reinbott, T.M.; Morris, R.O.
Plant Physiol. Biochem.
33
327-336
-
Endogenous cytokinin accumulation and cytokinin oxidase activity during shoot organogenesis of Petunia hybrida
1999
Auer, C.A.; Motyka, V.; Brezinova, A.; Kaminek, M.
Physiol. Plant.
105
141-147
-
Cytokinin oxidase - purification by affinity chromatography and activation by caffeic acid
1995
Wang, J.; Letham, D.S.
Plant Sci.
112
161-166
Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine
1999
Dobbek, H.; Gremer, L.; Meyer, O.; Huber, R.
Proc. Natl. Acad. Sci. USA
96
8884-8889
Identification of the prosthetic groups of dimethylamine dehydrogenase from Hyphomicrobium X
1979
Steenkamp, D.J.
Biochem. Biophys. Res. Commun.
88
244-250
Reaction of the C30A mutant of trimethylamine dehydrogenase with diethylmethylamine
1996
Huang, L.; Scrutton, N.S.; Hille, R.
J. Biol. Chem.
271
13401-13406
The reaction of phenylhydrazine with trimethylamine dehydrogenase and with free flavins
1979
Nagy, J.; Kenney, W.C.; Singer, T.P.
J. Biol. Chem.
254
2684-2688
Amino acid sequence of a cofactor peptide from trimethylamine dehydrogenase
1978
Kenney, W.C.; McIntire, W.; Steenkamp, D.J.
FEBS Lett.
85
137-140
Structure of the covalently bound coenzyme of trimethylamine dehydrogenase
1978
Steenkamp, D.J.; McIntire, W.; Kenney, W.C.
J. Biol. Chem.
253
2818-2824
A novel type of covalently bound coenzyme in the trimethylamine dehydrogenase
1978
Steenkamp, D.J.; Kenney, W.C.; Singer, T.P.
J. Biol. Chem.
253
2812-2817
Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase on catalysis
1978
Steenkamp, D.J.; Singer, T.P.; Beinert, H.
Biochem. J.
169
361-369
Identification of the iron-sulfur center in trimethylamine dehydrogenase
1977
Hill, C.L.; Steenkamp, D.J.; Holm, R.H.; Singer, T.P.
Proc. Natl. Acad. Sci. USA
74
547-551
-
Trimethylamine dehydrogenase from a methylotrophic bacterium. I. Isolation and steady-state kinetics
1976
Steenkamp, D.J.; Mallinson, J.
Biochim. Biophys. Acta
429
7005-719
Enzymological aspects of the pathways for the trimethylamine oxidation and C1 assimilation in obligate methylotrophs and restricted faculatative methylotrophs
1975
Colby, J.; Zatman, L.J.
Biochem. J.
148
513-520
Purification and properties of the trimethylamine dehydrogenase of bacterium 4B6
1974
Colby, J.; Zatman, L.J.
Biochem. J.
143
555-567
-
Crystal structure study of trimethylamine dehydrogenase
1985
Mathews, F.S.; Lim, L.W.; Shamala, N.
Flavins and Flavoproteins (Proc. Int. Symp. , 8th, Meeting Date 1984, 233-6, Bray, R. C. ; Engel, P. C. ; de Gruyter, M. S. G. eds. )
102
162926
-
Characterization of purified nitrate reductase A and chlorate reductase C from Proteus mirabilis
1976
Oltmann, L.F.; Reijnders, W.N.M.; Stouthamer, A.H.
Arch. Microbiol.
1111
25-35
Influence of tungstate on the formation and activities of four reductases in Proteus mirabilis: identification of two new molybdo-enzymes: chlorate reductase and tetrathionate reductase
1979
Oltmann, L.F.; Claassen, V.P.; Kastelein, P.; Reijnders, W.N.M.; Stouthamer, A.H.
FEBS Lett.
106
43-46
Study of chlorate-resistant mutants in Escherichia coli K 12
1971
Azoulay, E.; Mutaftschiev, S.; Rosado de Sousa, M.L.M.
Biochim. Biophys. Acta
237
579-590
-
Chlorate and nitrate reduction in the phototrophic bacteria Rhodobacter capsulatus and Rhodobacter sphaeroides
1994
Roldan, M.D.; Reyes, F.; Moreno-Vivian, C.; Castillo, F.
Curr. Microbiol.
29
241-245
Purification and characterization of (per)chlorate reductase from the chlorate-respiring strain GR-1
1999
Kengen, S.W.M.; Rikken, G.B.; Hagen, W.R.; Van Ginkel, C.G.; Stams, A.J.M.
J. Bacteriol.
181
6706-6711
Perchlorate and nitrate reductase activity in the perchlorate-respiring bacterium perclace
2001
Giblin, T.; Frankenberger, W.T., Jr.
Microbiol. Res.
156
311-315
-
Purification and characterization of nicotinic acid dehydrogenase from Pseudomonas fluorescens TN5
1994
Hurh, B.; Yamane, T.; Nagasawa, T.
J. Ferment. Bioeng.
78
19-26
Oxidation of nicotinic acid by a Bacillus species: purification and properties of nicotinic acid and 6-hydroxynicotinic acid hydroxylases
1971
Hirschberg, R.; Ensign, J.C.
J. Bacteriol.
108
751-756
-
Molybdenum-dependent degradation of nicotinic acid by Bacillus sp. DSM 2923
1989
Nagel, M.; Andreesen, J.R.
FEMS Microbiol. Lett.
59
147-152
-
Purification and characterization of the molybdoenzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini
1990
Nagel, M.; Andreesen, J.R.
Arch. Microbiol.
154
605-613
Selenium-containing xanthine dehydrogenase from Eubacterium barkeri
1999
Schräder, T.; Rienhöfer, A.; Andreesen, J.R.
Eur. J. Biochem.
264
862-871
-
Purification and some properties of xanthine dehydrogenase from wheat leaves
1998
Montalbini, P.
Plant Sci.
134
89-102
Effects of limited proteolysis on the structure and activity of turkey liver xanthine dehydrogenase
1977
Fhaolain, I.N.; Coughlan, M.P.
Biochem. Soc. Trans.
5
1705-1707
-
Use of rosy mutant strains of Drosophila melanogaster to probe the structure and function of xanthine dehydrogenase
1992
Hughes, R.K.; Doyle, W.A.; Chovnick, A.; Whittle, J.R.S.; Burke, J.F.; Bray, R.C.
Biochem. J.
285
507-513
Purification and properties of chicken liver xanthine dehydrogenase
1967
Rajagopalan, K.V.; Handler, P.
J. Biol. Chem.
242
4097-4107
Purification and properties of the NAD+-dependent (type D) and O2-dependent (type O) forms of rat liver xanthine dehydrogenase
1976
Waud, W.R.; Rajagopalan, K.V.
Arch. Biochem. Biophys.
172
354-364
Purification and properties of xanthine dehydrogenase from Pseudomonas acidovorans
1975
Sin, I.L.
Biochim. Biophys. Acta
410
12-20
Purification and characterization of a prokaryotic xanthine dehydrogenase from Comamonas acidovorans
1996
Xiang, Q.; Edmondson, D.E.
Biochemistry
35
5441-5450
Properties of xanthine dehydrogenase variants from rosy mutant strains of Drosophila melanogaster and their relevance to the enzyme's structure and mechanism
1996
Doyle, W.A.; Burke, J.F.; Chovnick, A.; Dutton, F.L.; Whittle, J.R.S.; Bray, R.C.
Eur. J. Biochem.
239
782-795
The mechanism of conversion of rat liver xanthine dehydrogenase from an NAD+-dependent form (type D) to an O2-dependent form (type O)
1976
Waud, W.R.; Rajagopalan, K.V.
Arch. Biochem. Biophys.
172
365-379
Purification and substrate inactivation of xanthine dehydrogenase from Chlamydomonas reinhardtii
1992
Perez-Vicente, R.; Alamillo, J.M.; Cardenas, J.; Pineda, M.
Biochim. Biophys. Acta
1117
159-166
Xanthine dehydrogenase from Drosophila melanogaster: Purification and properties of the wild-type enzyme and of a variant lacking iron-sulfur centers
1992
Hughes, R.K.; Bennett, B.; Bray, R.C.
Biochemistry
31
3073-3083
Regulation, purification, and properties of xanthine dehydrogenase in Neurospora crassa
1978
Lyon, E.S.; Garrett, R.H.
J. Biol. Chem.
253
2604-2614
Enzymes responsible for chlorate reduction by Pseudomonas sp. are different from those used for perchlorate reduction by Azospira sp
2005
Steinberg, L.M.; Trimble, J.J.; Logan, B.E.
FEMS Microbiol. Lett.
247
153-159
Moth desaturase characterized that produces both Z and E isomers of DELTA11-tetradecenoic acids
2002
Liu, W.; Jiao, H.; O'Connor, M.; Roelofs, W.L.
Insect Biochem. Mol. Biol.
32
1489-1495
Characterization of the chlorate reductase from Pseudomonas chloritidismutans
2003
Wolterink, A.F.; Schiltz, E.; Hagedoorn, P.L.; Hagen, W.R.; Kengen, S.W.; Stams, A.J.
J. Bacteriol.
185
3210-3213
Characterization of Z/E11- and Z9-desaturases from the obliquebanded leafroller moth, Choristoneura rosaceana
2002
Hao, G.; O'Connor, M.; Liu, W.; Roelofs, W.L.
J. Insect Sci.
2
26
Expression of recombinant membrane-bound type I iodothyronine deiodinase in yeast
2005
Kuiper, G.G.; Klootwijk, W.; Visser, T.J.
J. Mol. Endocrinol.
34
865-878
The C subunit of Ideonella dechloratans chlorate reductase: expression, purification, refolding, and heme reconstitution
2005
Karlsson, J.; Nilsson, T.
Protein Expr. Purif.
41
306-312
-
Bioluminescence activity of Latia luciferin analogues: replacement of the 2,6,6-trimethylcyclohexene ring onto the methyl-substituted phenyl groups
2004
Nakamura, M.; Mamino, M.; Masaki, M.; Maki, S.; Matsui, R.; Kojima, S.; Hirano, T.; Ohmiya, Y.; Niwa, H.
Tetrahedron Lett.
46
53-56
-
Bioluminescence in the limpet-like snail, Latia neritoides
2005
Ohmiya, Y.; Kojima, S.; Nakamura, M.; Niwa, H.
Bull. Chem. Soc. Jpn
78
1197-1205
Isolation and characterization of Alicycliphilus denitrificans strain BC, which grows on benzene with chlorate as the electron acceptor
2008
Weelink, S.A.; Tan, N.C.; ten Broeke, H.; van den Kieboom, C.; van Doesburg, W.; Langenhoff, A.A.; Gerritse, J.; Junca, H.; Stams, A.J.
Appl. Environ. Microbiol.
74
6672-6681
(Per)chlorate reduction by an acetogenic bacterium, Sporomusa sp., isolated from an underground gas storage
2010
Balk, M.; Mehboob, F.; van Gelder, A.H.; Rijpstra, W.I.; Damste, J.S.; Stams, A.J.
Appl. Microbiol. Biotechnol.
88
595-603
Mechanistic investigation of cPMP synthase in molybdenum cofactor biosynthesis using an uncleavable substrate analogue
2015
Hover, B.M.; Lilla, E.A.; Yokoyama, K.
Biochemistry
54
7229-7236
C-Terminal glycine-gated radical initiation by GTP 3',8-cyclase in the molybdenum cofactor biosynthesis
2015
Hover, B.M.; Yokoyama, K.
J. Am. Chem. Soc.
137
3352-3359
Mechanism of pyranopterin ring formation in molybdenum cofactor biosynthesis
2015
Hover, B.M.; Tonthat, N.K.; Schumacher, M.A.; Yokoyama, K.
Proc. Natl. Acad. Sci. USA
112
6347-6352
-
Sirohydrochlorin, a precursor of factor F430 biosynthesis in Methanobacterium thermoautotrophicum
1985
Mucha, H.; Keller, E.; Weber, H.; Lingens, F.; Troesch, W.
FEBS Lett.
190
169-171
The biosynthetic pathway of coenzyme F430 in methanogenic and methanotrophic Archaea
2016
Zheng, K.; Ngo, P.; Owens, V.; Yang, X.; Mansoorabadi, S.
Science
354
339-342
Genetic dissection of cyclic pyranopterin monophosphate biosynthesis in plant mitochondria
2018
Kruse, I.; Maclean, A.E.; Hill, L.; Balk, J.
Biochem. J.
475
495-509
Possible involvement of a tetrathionate reductase homolog in dissimilatory arsenate reduction by Anaeromyxobacter sp. strain PSR-1
2020
Muramatsu, F.; Tonomura, M.; Yamada, M.; Kasahara, Y.; Yamamura, S.; Iino, T.; Amachi, S.
Appl. Environ. Microbiol.
86
e00829-20
TsdC, a unique lipoprotein from Wolinella succinogenes that enhances tetrathionate reductase activity of TsdA
2017
Kurth, J.M.; Schuster, A.; Seel, W.; Herresthal, S.; Simon, J.; Dahl, C.
FEMS Microbiol. Lett.
364
fnx003
Heme ligation and redox chemistry in two bacterial thiosulfate dehydrogenase (TsdA) enzymes
2019
Jenner, L.P.; Kurth, J.M.; van Helmont, S.; Sokol, K.P.; Reisner, E.; Dahl, C.; Bradley, J.M.; Butt, J.N.; Cheesman, M.R.
J. Biol. Chem.
294
18002-18014
more
Show all BRENDA pathways known for reduced electron acceptor
close all tables 
open all tables
top
