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Information on EC 1.7.6.1 - nitrite dismutase and Organism(s) Rhodnius prolixus and UniProt Accession Q94734

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IUBMB Comments
Contains ferriheme b. The enzyme is one of the nitrophorins from the salivary gland of the blood-feeding insect Rhodnius prolixus. Nitric oxide produced induces vasodilation after injection. Nitrophorins 2 and 4 can also catalyse this reaction.
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Rhodnius prolixus
UNIPROT: Q94734
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The taxonomic range for the selected organisms is: Rhodnius prolixus
The expected taxonomic range for this enzyme is: Rhodnius prolixus
Reaction Schemes
hide
3
nitrite
+
2
H+
=
2
nitric oxide
+
nitrate
+
H2O
3
+
2
=
2
+
+
Synonyms
nitrophorin 4, nitrophorin 7, nitrite dismutase, prolixin s, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Nitrophorin 7
Prolixin S
SYSTEMATIC NAME
IUBMB Comments
nitrite:nitrite oxidoreductase
Contains ferriheme b. The enzyme is one of the nitrophorins from the salivary gland of the blood-feeding insect Rhodnius prolixus. Nitric oxide produced induces vasodilation after injection. Nitrophorins 2 and 4 can also catalyse this reaction.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3 nitrite + 2 H+
2 nitric oxide + nitrate + H2O
show the reaction diagram
3 nitrite + 2 H+
2 nitric oxide + nitrate + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3 nitrite + 2 H+
2 nitric oxide + nitrate + H2O
show the reaction diagram
3 nitrite + 2 H+
2 nitric oxide + nitrate + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme
the crystal structure of NP4 reveals a lipocalin-like eight-stranded beta barrel, with heme inserted into one end of the barrel
heme b
heme b
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.72
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
NP7 inhibits prothrombin activation by blocking phospholipid binding sites for the prothrombinase complex on the surfaces of vesicles and activated platelets. As a NO complex, NP7 inhibits collagen and ADP-induced platelet aggregation and induces disaggregation of ADP-stimulated platelets by an NO-mediated mechanism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NP4_RHOPR
205
1
22406
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20600
x * 20600, calculated from sequence
20966
x * 20966, MALDI-TOF-MS
20969
x * 20969, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of nitrophorin 4 at 1.5 A resolution
protein crystals are obtained using the vapor diffusion method with the conditions containing 3.2 M ammonium phosphate (pH 7.4). X-ray crystallography of NP4 crystals soaked with nitrite reveals the formation of an eta1-N nitro complex
mutant enzyme E27V, vapor diffusion method, using 0.33% (w/v) anthrone, 0.33% (w/v) Congo Red, 0.33% (w/v) N-(2-acetamido)-2-aminoethanesulfonic acid, 0.0 2M HEPES sodium pH 6.8
solid-state NMR analysis. Enzyme tends to form oligomers and precipitates at higher concentration. At concentrations of approximately 0.1-2 mM oligomers are in equilibrium with monomers. The protein oligomerizes preferably in units of trimers, hexamers, and higher oligomeric states of unidentified composition
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E27Q
the mutation results in progressive loss of the characteristic pH sensitivity of the ligand binding rate observed for the wild type protein
E27V
the mutation results in progressive loss of the characteristic pH sensitivity of the ligand binding rate observed for the wild type protein
K149A
using 3:1 phosphatidylcholine:phosphatidylserine vesicles, binding is reduced by a factor of three from that observed with wild-type protein, suggesting that this region does play an important role in phospholipid binding
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 5
the enzyme-NO complex is more stable at pH 4-5 than at physiologic pH. pH. In pH 4.5 sodium acetate buffer, a complex formed by incubation with S-nitroso-N-acetylpenicillamine is stable for several hours at room temperature, is purified by gel filtration chromatography at pH 4.5, and maintains indefinitely at -20°C. Raising the pH of the complex solution by adding concentrated Tris-HCl, pH 7.5 results in dissociation of the complex over a period of 10-15 min
714157
7.5
the enzyme-NO complex is more stable at pH 4-5 than at physiologic pH. pH. In pH 4.5 sodium acetate buffer, a complex formed by incubation with S-nitroso-N-acetylpenicillamine is stable for several hours at room temperature, is purified by gel filtration chromatography at pH 4.5, and maintains indefinitely at -20°C. Raising the pH of the complex solution by adding concentrated Tris-HCl, pH 7.5 results in dissociation of the complex over a period of 10-15 min
714157
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
truncated mutant enzyme NP7(DELTA1-3) shows marked decay above 45°C. Wild-type nitrophorin 7, in contrast, is comparatively stable, and does not experience a marked signal decrease of activity at temperatures below 52 °C
52
truncated mutant enzyme NP7(DELTA1-3) shows marked decay above 45°C. Wild-type nitrophorin 7, in contrast, is comparatively stable, and does not experience a marked signal decrease of activity at temperatures below 52 °C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NP7 is unstable when lyophilized
the N-terminus of NP7 significantly stabilizes the protein fold
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the NP7 protein is obtained as inclusion bodies and is denatured, refolded, and reconstituted with heme as described for other nitrophorins. The refolded reconstituted protein is purified by a two-step procedure
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)
expression in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)
expression in Escherfichia coli
expression in Escherichia coli BL21. Expression and reconstitution method for NP7 that yields sufficient amounts of pure protein for extensive characterization
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Andersen, J.F.; Gudderra, N.P.; Francischetti, I.M.; Valenzuela, J.G.; Ribeiro, J.M.
Recognition of anionic phospholipid membranes by an antihemostatic protein from a blood-feeding insect
Biochemistry
43
6987-6994
2004
Rhodnius prolixus (Q6PQK2)
Manually annotated by BRENDA team
Knipp, M.; Yang, F.; Berry, R.E.; Zhang, H.; Shokhirev, M.N.; Walker, F.A.
Spectroscopic and functional characterization of nitrophorin 7 from the blood-feeding insect Rhodnius prolixus reveals an important role of its isoform-specific N-terminus for proper protein function
Biochemistry
46
13254-13268
2007
Rhodnius prolixus (Q6PQK2), Rhodnius prolixus
Manually annotated by BRENDA team
He, C.; Ogata, H.; Knipp, M.
Formation of the complex of nitrite with the ferriheme b beta-barrel proteins nitrophorin 4 and nitrophorin 7
Biochemistry
49
5841-5851
2010
Rhodnius prolixus (Q6PQK2), Rhodnius prolixus (Q94734), Rhodnius prolixus
Manually annotated by BRENDA team
He, C.; Knipp, M.
Formation of nitric oxide from nitrite by the ferriheme b protein nitrophorin 7
J. Am. Chem. Soc.
131
12042-12043
2009
Rhodnius prolixus (Q6PQK2), Rhodnius prolixus (Q94734)
Manually annotated by BRENDA team
Knipp, M.; Zhang, H.; Berry, R.E.; Walker, F.A.
Overexpression in Escherichia coli and functional reconstitution of the liposome binding ferriheme protein nitrophorin 7 from the bloodsucking bug Rhodnius prolixus
Protein Expr. Purif.
54
183-191
2007
Rhodnius prolixus (Q6PQK2), Rhodnius prolixus
Manually annotated by BRENDA team
Andersen, J.F.; Weichsel, A.; Balfour, C.A.; Champagne, D.E.; Montfort, W.R.
The crystal structure of nitrophorin 4 at 1.5 A resolution: transport of nitric oxide by a lipocalin-based heme protein
Structure
6
1315-1327
1998
Rhodnius prolixus (Q94734), Rhodnius prolixus
Manually annotated by BRENDA team
Varghese, S.; Yang, F.; Pacheco, V.; Wrede, K.; Medvedev, A.; Ogata, H.; Knipp, M.; Heise, H.
Expression, purification and solid-state NMR characterization of the membrane binding beme protein nitrophorin 7 in two electronic spin states
Biochemistry
52
7031-7040
2013
Rhodnius prolixus (Q6PQK2), Rhodnius prolixus
Manually annotated by BRENDA team
Abbruzzetti, S.; Allegri, A.; Bidon-Chanal, A.; Ogata, H.; Soavi, G.; Cerullo, G.; Bruno, S.; Montali, C.; Luque, F.J.; Viappiani, C.
Electrostatic tuning of the ligand binding mechanism by Glu27 in nitrophorin 7
Sci. Rep.
8
10855
2018
Rhodnius prolixus (Q6PQK2), Rhodnius prolixus
Manually annotated by BRENDA team