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Information on EC 1.6.3.5 - renalase and Organism(s) Mus musculus and UniProt Accession A7RDN6

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EC Tree
     1 Oxidoreductases
         1.6 Acting on NADH or NADPH
             1.6.3 With oxygen as acceptor
                1.6.3.5 renalase
IUBMB 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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Mus musculus
UNIPROT: A7RDN6
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
renalase, ren-2, ren-1, renalase-1, more
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-NADH + H+ + O2
beta-NAD+ + H2O2
show the reaction diagram
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
substantial expression cortex of adrenal gland
Manually annotated by BRENDA team
substantial expression in granulosa
Manually annotated by BRENDA team
substantial expression in oocytes
Manually annotated by BRENDA team
substantial expression in interstitial and luteal cells of ovary. Expression increases in testes and ovaries as mice develop and is further enhanced in the ovaries of pregnant mice
Manually annotated by BRENDA team
substantial expression spermatogenic cells of testis. Expression increases in testes and ovaries as mice develop
Manually annotated by BRENDA team
additional information
renalase is predominantly expressed in reproductive/steroidogenic systems, with particularly substantial expression in oocytes, granulosa, interstitial and luteal cells of ovary, spermatogenic cells of testis, and cortex of adrenal gland
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
genetic deletion of renalase results in more severe disease in murine models of acute pancreatitis, and administering recombinant RNLS to cerulein-exposed wild-type mice after pancreatitis onset is protective. Plasma membrane calcium ATPase 4b is expressed in both murine and human acinar cells and a PMCA4b-selective inhibitor worsens pancreatitis-induced injury and blocks the protective effects of rcombinant RNLS
physiological function
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renalase knockout mouse model to explore the mechanisms mediating renalase's effect on phosphate excretion. Compared with wild-type mice maintained on a regular diet, knockout mice show decreased serum phosphate and increased urinary phosphate excretion. Both wild-type and knocout mice respond similarly to phosphate restriction by increasing renal catechol-O-methyl transferase COMT-1 activity and markedly decreasing phosphate excretion. Only catechol-O-methyl transferase expression and activity are significantly increased in knockout mice. Urinary dopamine increases by twofold, whereas urinary l-DOPA excretion decreases by twofold in the knockout mouse
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RNLS_MOUSE
342
0
37597
Swiss-Prot
Secretory Pathway (Reliability: 3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gonadotropin-releasing hormone antagonist, cetrorelix, represses renalase expression in mice ovaries and testes
knockout of leptin, an effector and modulator of steroid hormones and reproduction, causes a dramatic increase of renalase expression in mice testes
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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renalase deficiency is associated with increased renal dopamine synthesis, stimulated phosphate excretion, and moderately severe hypophosphatemia. The signal to increase renal dopamine synthesis is strong since it overcomes a compensatory increase in catechol-O-methyl transferase activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kolodecik, T.R.; Reed, A.M.; Date, K.; Shugrue, C.A.; Patel, V.; Chung, S.L.; Desir, G.V.; Gorelick, F.S.
The serum protein renalase reduces injury in experimental pancreatitis
J. Biol. Chem.
292
21047-21059
2017
Mus musculus (A7RDN6), Homo sapiens (Q5VYX0)
Manually annotated by BRENDA team