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Information on EC 1.11.1.7 - peroxidase and Organism(s) Sorghum bicolor and UniProt Accession P84516

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.7 peroxidase
IUBMB Comments
Heme proteins with histidine as proximal ligand. The iron in the resting enzyme is Fe(III). They also peroxidize non-phenolic substrates such as 3,3',5,5'-tetramethylbenzidine (TMB) and 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS). Certain peroxidases (e.g. lactoperoxidase, SBP) oxidize bromide, iodide and thiocyanate.
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This record set is specific for:
Sorghum bicolor
UNIPROT: P84516
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Word Map
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The taxonomic range for the selected organisms is: Sorghum bicolor
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
2
phenolic donor
+
H2O2
=
2
phenoxyl radical of the donor
+
2
H2O
2
phenolic donor
+
=
2
phenoxyl radical of the donor
+
2
Synonyms
horseradish peroxidase, horseradish peroxidase (hrp), rhepo, lactoperoxidase, eosinophil peroxidase, guaiacol peroxidase, heme peroxidase, rubrerythrin, cyp119, thiol peroxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
eosinophil peroxidase
-
-
-
-
extensin peroxidase
-
-
-
-
guaiacol peroxidase
-
-
-
-
heme peroxidase
-
-
-
-
horseradish peroxidase (HRP)
-
-
-
-
Japanese radish peroxidase
-
-
-
-
lactoperoxidase
-
-
-
-
MPO
-
-
-
-
myeloperoxidase
-
-
-
-
oxyperoxidase
-
-
-
-
protoheme peroxidase
-
-
-
-
pyrocatechol peroxidase
-
-
-
-
scopoletin peroxidase
-
-
-
-
thiocyanate peroxidase
-
-
-
-
verdoperoxidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
phenolic donor:hydrogen-peroxide oxidoreductase
Heme proteins with histidine as proximal ligand. The iron in the resting enzyme is Fe(III). They also peroxidize non-phenolic substrates such as 3,3',5,5'-tetramethylbenzidine (TMB) and 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS). Certain peroxidases (e.g. lactoperoxidase, SBP) oxidize bromide, iodide and thiocyanate.
CAS REGISTRY NUMBER
COMMENTARY hide
9003-99-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ferulic acid + H2O2
?
show the reaction diagram
-
-
-
?
indole-3-acetic acid + H2O2
?
show the reaction diagram
-
-
-
?
N-acetyl-L-tyrosine + H2O2
?
show the reaction diagram
-
-
-
?
N-acetyl-L-tyrosine methyl ester + H2O2
?
show the reaction diagram
-
-
-
?
p-coumaric acid + H2O2
?
show the reaction diagram
-
-
-
?
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O
show the reaction diagram
-
-
-
?
2 guaiacol + H2O2
3,3'-dimethoxy-4,4'-biphenylquinone + H2O
show the reaction diagram
-
27% of the activity with 2,4-dichlorophenol
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme
the enzyme contains a type-b heme
heme
-
enzyme contains a high-spin heme. The FeIII/FeII reduction potential is -266 mV vs normal hydrogen electrode. The gamma-heme edge shows a substrate binding site
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
SPC4 is activated by Ca2+. Ca2+-binding increases the protein conformational stability by raising the melting temperature from 67°C to 82°C
Iron
-
enzyme contains a high-spin heme. The FeIII/FeII reduction potential is -266 mV vs normal hydrogen electrode. The ferric enzyme binds cyanide or azide to give a low-spin species
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
about 8fold increase in kcat value in presence of Ca2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6
H2O2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.9 - 87
H2O2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8
reaction with reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid)
5.5
reaction with ferulic acid
6.5
reaction with N-acetyl-L-tyrosine
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Moench var. Cauga 108–15
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PER1_SORBI
362
0
38452
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
gel filtration
38000
1 * 38000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
SPC4 consists of two glycoforms with molecular masses of 34227 Da and 35629 Da. Sugar contents of 3.0% w/w and 6.7% w/w in glycoform I and II, respectively, and a mass of the apoprotein of 33 246 Da. The glycosylation sites of SPC4 are localized in the C-terminus part of the enzyme. Main sugar constituents of the glycan chains are fucose, mannose, xylose, and N-acetylglucosamine
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.27 A resolution. Metal binding sites are observed in the structure on the distal (assigned as a Na+ ion) and proximal (assigned as a Ca2+) sides of the heme
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 7
25°C, 2 h, stable
673542
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
in the absence of added CaCl2, SPC4 readily loses activity when incubated at temperatures above 55°C
67
Ca2+-binding increases the protein conformational stability by raising the melting temperature from 67°C to 82°C
82
Ca2+-binding increases the protein conformational stability by raising the melting temperature from 67°C to 82°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+-binding increases the protein conformational stability by raising the melting temperature from 67°C to 82°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dicko, M.H.; Gruppen, H.; Hilhorst, R.; Voragen, A.G.; van Berkel, W.J.
Biochemical characterization of the major Sorghum grain peroxidase
FEBS J.
273
2293-2307
2006
Sorghum bicolor (P84516)
Manually annotated by BRENDA team
Nnamchi, C.I.; Parkin, G.; Efimov, I.; Basran, J.; Kwon, H.; Svistunenko, D.A.; Agirre, J.; Okolo, B.N.; Moneke, A.; Nwanguma, B.C.; Moody, P.C.; Raven, E.L.
Structural and spectroscopic characterisation of a heme peroxidase from sorghum
J. Biol. Inorg. Chem.
21
63-70
2016
Sorghum bicolor, Sorghum bicolor SK 5912
Manually annotated by BRENDA team