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1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
2-dihydronicotinamide adenine dinucleotide phosphate + O2
?
-
-
-
?
2-dihydronicotinamide riboside + O2
?
-
-
-
?
6-dihydronicotinamide adenine dinucleotide phosphate + O2
?
-
-
-
?
6-dihydronicotinamide riboside + O2
?
-
-
-
?
alpha-NAD(P)H + H+ + O2
beta-NAD(P)+ + H2O2
alpha-NADH + H+ + O2
beta-NAD+ + H2O2
alpha-NADPH + H+ + O2
beta-NADP+ + H2O2
catecholamine + O2
oxidized catecholamine + H2O2
-
-
-
?
catecholamine + O2
oxidized catecholamine + NH3 + H2O2
-
-
-
?
dopamine + O2
?
-
-
-
-
?
epinephrine + O2
?
-
-
-
-
?
NAD(P)H + H+ + tetrazolium
NAD(P)+ + formazan
-
-
-
?
nephrine + O2
?
-
-
-
-
?
Norepinephrine + O2
?
-
-
-
-
?
additional information
?
-
1,2-dihydro-beta-NADH + H+ + O2

beta-NAD+ + H2O2
-
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2

beta-NADP+ + H2O2
-
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2

beta-NAD+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2

beta-NADP+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
-
?
alpha-NAD(P)H + H+ + O2

beta-NAD(P)+ + H2O2
-
renalase is selective for the alpha-anomer, which binds with a dissociation constant of about 20 microM. This association precedes monophasic two-electron reduction of the FAD cofactor with a rate constant of 40.2 per s. The reduced enzyme then delivers both electrons to dioxygen in a second-order reaction with a rate constant of about 2900 per M and s. Renalase has modest affinity for its beta-NADP+ product, and the FAD cofactor has a reduction potential of -155 mV that is unaltered by saturating beta-NADP+. Data suggest that the products are formed and released in a kinetically ordered sequence, first beta-NADP+ then H2O2
-
?
alpha-NAD(P)H + H+ + O2
beta-NAD(P)+ + H2O2
renalase is a protein hormone secreted into the blood by the kidney that is reported to lower blood pressure and slow heart rate
-
-
?
alpha-NAD(P)H + H+ + O2
beta-NAD(P)+ + H2O2
the substrate alpha-dihydropyridyl ring is oxidized by transferring two electrons to the flavin cofactor and the configuration of the ribose C1 is converted from alpha to beta. The reduced FAD cofactor then reoxidizes by reacting with dioxygen to yield hydrogen peroxide
-
-
?
alpha-NADH + H+ + O2

beta-NAD+ + H2O2
-
-
-
-
?
alpha-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
alpha-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
-
?
alpha-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
-
?
alpha-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
alpha-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
alpha-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
alpha-NADPH + H+ + O2

beta-NADP+ + H2O2
-
-
-
-
?
alpha-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
alpha-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
-
?
alpha-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
alpha-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
additional information

?
-
renalase has an extremely low diaphorase activity, displaying lower kcat but higher kcat/Km for NADH compared to NADPH
-
-
?
additional information
?
-
-
renalase has an extremely low diaphorase activity, displaying lower kcat but higher kcat/Km for NADH compared to NADPH
-
-
?
additional information
?
-
-
renalase does not catalyze the oxidation of catecholamines
-
-
?
additional information
?
-
renalase exhibits a preference for substrates derived from beta-NAD+ over those derived from beta-NADP+
-
-
?
additional information
?
-
renalase exhibits a preference for substrates derived from beta-NAD+ over those derived from beta-NADP+
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
alpha-NAD(P)H + H+ + O2
beta-NAD(P)+ + H2O2
renalase is a protein hormone secreted into the blood by the kidney that is reported to lower blood pressure and slow heart rate
-
-
?
alpha-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
alpha-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
catecholamine + O2
oxidized catecholamine + H2O2
-
-
-
?
dopamine + O2
?
-
-
-
-
?
epinephrine + O2
?
-
-
-
-
?
nephrine + O2
?
-
-
-
-
?
Norepinephrine + O2
?
-
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2

beta-NAD+ + H2O2
-
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
-
?
1,2-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2

beta-NADP+ + H2O2
-
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
-
?
1,2-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2

beta-NAD+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADH + H+ + O2
beta-NAD+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2

beta-NADP+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
-
?
1,6-dihydro-beta-NADPH + H+ + O2
beta-NADP+ + H2O2
-
-
-
-
?
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.
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.
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.
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.
Beaupre, B.A.; Carmichael, B.R.; Hoag, M.R.; Shah, D.D.; Moran, G.R.
Renalase is an alpha-NAD(P)H oxidase/anomerase
J. Am. Chem. Soc.
135
13980-13987
2013
Homo sapiens (Q5VYX0)
brenda
Sizova, D.; Velazquez, H.; Sampaio-Maia, B.; Quelhas-Santos, J.; Pestana, M.; Desir, G.V.
Renalase regulates renal dopamine and phosphate metabolism
Am. J. Physiol. Renal Physiol.
305
F839-F844
2013
Mus musculus
brenda
Beaupre, B.A.; Hoag, M.R.; Carmichael, B.R.; Moran, G.R.
Kinetics and equilibria of the reductive and oxidative half-reactions of human renalase with alpha-NADPH
Biochemistry
52
8929-8937
2013
Homo sapiens (Q5VYX0), Homo sapiens
brenda
Xu, J.; Li, G.; Wang, P.; Velazquez, H.; Yao, X.; Li, Y.; Wu, Y.; Peixoto, A.; Crowley, S.; Desir, G.V.
Renalase is a novel, soluble monoamine oxidase that regulates cardiac function and blood pressure
J. Clin. Invest.
115
1275-1280
2005
Rattus norvegicus (Q5U2W9), Homo sapiens (Q5VYX0), Homo sapiens
brenda
Milani, M.; Ciriello, F.; Baroni, S.; Pandini, V.; Canevari, G.; Bolognesi, M.; Aliverti, A.
FAD-binding site and NADP reactivity in human renalase: a new enzyme involved in blood pressure regulation
J. Mol. Biol.
411
463-473
2011
Homo sapiens (Q5VYX0), Homo sapiens
brenda
Zhou, M.; Liang, T.; Wang, Y.; Jin, D.; Wang, J.; Jia, L.; Zhang, S.
Expression and tissue localization of renalase, a novel soluble FAD-dependent protein, in reproductive/steroidogenic systems
Mol. Biol. Rep.
40
3987-3994
2013
Mus musculus (A7RDN6)
brenda
Quelhas-Santos, J.; Serrao, M.P.; Soares-Silva, I.; Fernandes-Cerqueira, C.; Simoes-Silva, L.; Pinho, M.J.; Remiao, F.; Sampaio-Maia, B.; Desir, G.V.; Pestana, M.
Renalase regulates peripheral and central dopaminergic activities
Am. J. Physiol. Renal Physiol.
308
F84-F91
2015
Mus musculus
brenda
Beaupre, B.A.; Hoag, M.R.; Moran, G.R.
Renalase does not catalyze the oxidation of catecholamines
Arch. Biochem. Biophys.
579
62-66
2015
Homo sapiens
brenda
Beaupre, B.A.; Roman, J.V.; Hoag, M.R.; Meneely, K.M.; Silvaggi, N.R.; Lamb, A.L.; Moran, G.R.
Ligand binding phenomena that pertain to the metabolic function of renalase
Arch. Biochem. Biophys.
612
46-56
2016
Pseudomonas savastanoi pv. phaseolicola (Q48MT7), Pseudomonas savastanoi pv. phaseolicola 1448A (Q48MT7)
brenda
Moran, G.R.; Hoag, M.R.
The enzyme Renalase
Arch. Biochem. Biophys.
632
66-76
2017
Pseudomonas savastanoi (Q48MT7), Homo sapiens (Q5VYX0), Pseudomonas savastanoi 1448A (Q48MT7)
brenda
Severina, I.; Fedchenko, V.; Veselovsky, A.; Medvedev, A.
The history of renalase from amine oxidase to alpha-NAD(P)H-oxidase/anomerase
Biochemistry (Moscow)
10
97-109
2016
Homo sapiens (Q5VYX0)
brenda
Sonawane, P.J.; Gupta, V.; Sasi, B.K.; Kalyani, A.; Natarajan, B.; Khan, A.A.; Sahu, B.S.; Mahapatra, N.R.
Transcriptional regulation of the novel monoamine oxidase renalase Crucial roles of transcription factors Sp1, STAT3, and ZBP89
Biochemistry
53
6878-6892
2014
Homo sapiens
brenda
Hoag, M.R.; Roman, J.; Beaupre, B.A.; Silvaggi, N.R.; Moran, G.R.
Bacterial renalase structure and kinetics of an enzyme with 2- and 6-dihydro-beta-NAD(P) oxidase activity from Pseudomonas phaseolicola
Biochemistry
54
3791-3802
2015
Pseudomonas syringae, Pseudomonas syringae 1448A
brenda
Beaupre, B.A.; Hoag, M.R.; Roman, J.; Foersterling, F.H.; Moran, G.R.
Metabolic function for human renalase oxidation of isomeric forms of beta-NAD(P)H that are inhibitory to primary metabolism
Biochemistry
54
795-806
2015
Homo sapiens
brenda
Moran, G.R.
The catalytic function of renalase A decade of phantoms
Biochim. Biophys. Acta
1864
177-186
2016
Homo sapiens (Q5VYX0), Homo sapiens
brenda
Quelhas-Santos, J.; Soares-Silva, I.; Fernandes-Cerqueira, C.; Simoes-Silva, L.; Ferreira, I.; Carvalho, C.; Coentrao, L.; Vaz, R.; Sampaio-Maia, B.; Pestana, M.
Plasma and urine renalase levels and activity during the recovery of renal function in kidney transplant recipients
Exp. Biol. Med. (Maywood)
239
502-508
2014
Homo sapiens
brenda
Fedchenko, V.I.; Buneeva, O.A.; Kopylov, A.T.; Veselovsky, A.V.; Zgoda, V.G.; Medvedev, A.E.
Human urinary renalase lacks the N-terminal signal peptide crucial for accommodation of its FAD cofactor
Int. J. Biol. Macromol.
78
347-353
2015
Homo sapiens (Q5VYX0), Homo sapiens
brenda
Wang, Y.; Safirstein, R.; Velazquez, H.; Guo, X.J.; Hollander, L.; Chang, J.; Chen, T.M.; Mu, J.J.; Desir, G.V.
Extracellular renalase protects cells and organs by outside-in signalling
J. Cell. Mol. Med.
21
1260-1265
2017
Homo sapiens
brenda
Li, X.; Xie, Z.; Lin, M.; Huang, R.; Liang, Z.; Huang, W.; Jiang, W.
Renalase protects the cardiomyocytes of Sprague-Dawley rats against ischemia and reperfusion injury by reducing myocardial cell necrosis and apoptosis
Kidney Blood Press. Res.
40
215-222
2015
Rattus norvegicus
brenda
Fedchenko, V.; Kopylov, A.; Kozlova, N.; Buneeva, O.; Kaloshin, A.; Zgoda, V.; Medvedev, A.
Renalase secreted by human kidney HEK293T cells lacks its n-terminal peptide implications for putative mechanisms of renalase action
Kidney Blood Press. Res.
41
593-603
2016
Homo sapiens
brenda
Li, X.; Huang, R.; Xie, Z.; Lin, M.; Liang, Z.; Yang, Y.; Jiang, W.
Renalase, a new secretory enzyme Its role in hypertensive-ischemic cardiovascular diseases
Med. Sci. Monit.
20
688-692
2014
Homo sapiens
brenda