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Information on EC 1.6.3.5 - renalase
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1.6.3.5 renalaseIUBMB Comments
Requires FAD. Renalase, previously thought to be a hormone, is a flavoprotein secreted into the blood by the kidney that oxidizes the 1,2-dihydro- and 1,6-dihydro- isomeric forms of beta-NAD(P)H back to beta-NAD(P)+. These isomeric forms, generated by nonspecific reduction of beta-NAD(P)+ or by tautomerization of beta-NAD(P)H, are potent inhibitors of primary metabolism dehydrogenases and pose a threat to normal respiration.
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Word Map
- 1.6.3.5
- hypertension
- renin
- angiotensin
-
renin-angiotensin
- cardiac
- catecholamine
-
normotensive
- cardiovascular
- arterial
- hypertrophy
-
sympathetic
-
systolic
-
glomerular
-
antihypertensive
- proteinuria
-
angiotensin-converting
-
hansd
-
hannover
- losartan
- glomerulosclerosis
- prorenin
-
tgrmren227
-
conscious
-
ii-dependent
- angiotensinogen
- endothelin
-
nephrectomized
-
transgene-negative
-
intrarenal
-
renoprotective
-
epoxyeicosatrienoic
-
end-organ
- perindopril
- bosentan
-
extra-renal
-
atrasentan
-
bp-lowering
-
aorto-caval
-
dinucleotide-dependent
-
prehypertensive
- medicine
- valsartan
-
monogenetic
-
juxtaglomerular
-
mren227
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
renalase, ren-2, ren-1, renalase-1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alphaNAD(P)H oxidase/anomerase
REN
renalase-1
RnlS
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1,2-dihydro-beta-NAD(P) + H+ + O2 = beta-NAD(P)+ + H2O2
(1)
-
-
-
1,6-dihydro-beta-NAD(P) + H+ + O2 = beta-NAD(P)+ + H2O2
(2)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
dihydro-NAD(P):oxygen oxidoreductase (H2O2-forming)
Requires FAD. Renalase, previously thought to be a hormone, is a flavoprotein secreted into the blood by the kidney that oxidizes the 1,2-dihydro- and 1,6-dihydro- isomeric forms of beta-NAD(P)H back to beta-NAD(P)+. These isomeric forms, generated by nonspecific reduction of beta-NAD(P)+ or by tautomerization of beta-NAD(P)H, are potent inhibitors of primary metabolism dehydrogenases and pose a threat to normal respiration.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-dihydronicotinamide adenine dinucleotide phosphate + O2
?
-
-
-
?
6-dihydronicotinamide adenine dinucleotide phosphate + 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-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-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-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+
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
-
-
?
1,6-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
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
flavoprotein. 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
FAD
the FAD cofactor has a reduction potential of ?155 mV that is unaltered by saturating beta-NADP+
FAD
the FAD prosthetic group becomes slowly reduced when the enzyme is incubated with NADPH under anaerobiosis
FAD
-
only extracellular (circulating) renalase acts in a FAD-independent manner
additional information
a recognizable NADP-binding site is absent in the protein structure, enzyme shows poor affinity for, and poor reactivity towards, NADH and NADPH with Kd values of ca 2 mM
-
additional information
-
a recognizable NADP-binding site is absent in the protein structure, enzyme shows poor affinity for, and poor reactivity towards, NADH and NADPH with Kd values of ca 2 mM
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
111
MBP-tagged mutant m6Ren1, pH not specified in the publication, temperature not specified in the publication
1447
mutant m5Ren1, pH not specified in the publication, temperature not specified in the publication
152
SUMO-tagged mutant m6Ren1, pH not specified in the publication, temperature not specified in the publication
19.8
MBP-tagged wild-type, pH not specified in the publication, temperature not specified in the publication
289
SUMO-tagged mutant m5Ren1, pH not specified in the publication, temperature not specified in the publication
63
SUMO-tagged wild-type, pH not specified in the publication, temperature not specified in the publication
760
mutant m6Ren1, pH not specified in the publication, temperature not specified in the publication
87.6
wild-type, pH not specified in the publication, temperature not specified in the publication
91
MBP-tagged mutant m5Ren1, pH not specified in the publication, temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE