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Information on EC 1.11.1.7 - peroxidase and Organism(s) Sulfolobus acidocaldarius and UniProt Accession Q55080
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1.11.1.7 peroxidaseIUBMB 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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Word Map
- 1.11.1.7
-
retrograde
-
dorsal
- nerve
- nuclei
-
medial
-
afferent
- fiber
-
tracer
- spinal
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ventral
-
ipsilateral
- cord
-
rostrally
-
innervation
-
contralateral
- dendrite
-
caudal
-
anterograde
- ganglion
- posterior
-
electrode
- agglutinin
- reticular
-
tracing
- erythropoietin
- peroxidases
- lamina
- motoneuron
- thalamic
-
trigeminal
-
geniculate
-
topographic
-
arbor
- colliculus
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dorsolateral
-
somata
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ventrolateral
-
boutons
- collateral
-
ventromedial
- commissure
-
vestibular
- pontine
-
dorsomedial
-
raphe
-
send
-
mesencephalic
-
iontophoretic
-
immunosensors
- tegmental
- analysis
- medicine
- nutrition
- degradation
- synthesis
- food industry
- agriculture
The taxonomic range for the selected organisms is: Sulfolobus acidocaldarius
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -
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
9003-99-0
-
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
AmplexRed + cumene hydroperoxide
?
the initial activity of CYP119 in the presence of cumene hydroperoxide is 5fold higher than that observed with H2O2
-
-
?
AmplexRed + tert-butyl hydroperoxide
?
the initial activity of CYP119 in the presence of tert-butyl hydroperoxide is 2fold higher than that observed with H2O2
-
-
?
cis-beta-methylstyrene + H2O
cis-beta-methylstyrene epoxide + H2O
epoxidation takes place with complete retention of the olefin stereochemistry
-
-
?
cis-stilbene + H2O
cis-stilbene epoxide + H2O
epoxidation takes place with complete retention of the olefin stereochemistry
-
-
?
styrene + H2O2
styrene epoxide + H2O
endogenous electron transfer partners for CYP119 remain unknown, highly unlikely that styrene is the natural substrate for CYP119. Catalytic activity can be assayed in the absence of electron donor proteins using H2O2 as the source of oxidizing equivalents. The enzyme is not able to support styrene epoxidation by putidaredoxin/putidaredoxin reductase
-
-
?
additional information
?
-
catalytic mechanism: Thr213 is catalytically important and Thr214 helps to control the iron spin state
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T213A
T213A/T214A
T213F
no formation of styrene epoxide. Protein melting temperature is 2.4°C lower compared to wild-type enzyme
T213S
formation of styrene epoxide is 19% compared to wild-type enzyme. Protein melting temperature is 2°C lower compared to wild-type enzyme
T213V
formation of styrene epoxide is 0.7% compared to wild-type enzyme. Protein melting temperature is 1.1°C lower compared to wild-type enzyme
T213W
T214A
formation of styrene epoxide is 2.7fold higher as compared to wild-type enzyme. Protein melting temperature is 1.6°C lower compared to wild-type enzyme
T214V
formation of styrene epoxide is 2.9fold higher as compared to wild-type enzyme. Protein melting temperature is 2.3°C higher as compared to wild-type enzyme. Mutant is separated into two distinct bands during chromatofocusing. The first band contains predominantly low spin protein, and the second band contains predominantly high spin protein
T213A
formation of styrene epoxide is 83% compared to wild-type enzyme. Protein melting temperature is 1.6°C lower compared to wild-type enzyme
T213A
the mutant enzyme shows an important red-shift of their fluorescence maximum, along with an increased shoulder at 396 nm, significant alteration in the protein structure, causing some of the tryptophan residues to become more solvent accessible
T213A/T214A
formation of styrene epoxide is 1.4fold higher as compared to wild-type enzyme. Protein melting temperature is 3.5°C higher as compared to wild-type enzyme
T213A/T214A
the mutant enzyme shows an important red-shift of their fluorescence maximum, along with an increased shoulder at 396 nm, significant alteration in the protein structure, causing some of the tryptophan residues to become more solvent accessible
T213W
formation of styrene epoxide is 5% compared to wild-type enzyme. Protein melting temperature is 2.4°C lower compared to wild-type enzyme
T213W
the fluorescence yield of the T213W mutant enzyme is slightly lower than that of the wild type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
87
protein melting temperature of mutant enzyme T213A/T214A is 87.0°C
88
protein melting temperature of mutant enzymes T213F and T213W is 88.1°C
89
protein melting temperature of mutant enzymes T213A and T214A is 88.9°C, protein melting temperature of mutant enzyme T213V is 89.4°C, protein melting temperature of mutant enzyme T213S is 88.5°C
91
protein melting temperature of wild-type enzyme is 90.5°C
93
protein melting temperature of mutant enzyme T214V is 92.8°C
additional information
protein melting curves indicate that the thermal stability of CYP119 does not depend on the iron spin state or the active site architecture defined by the threonine residues
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
pressure stability of the wild-type enzyme and its active-site Thr213 and Thr214 mutants is investigated. The protein is reversibly inactivated by pressure. At 20°C and pH 6.5, the protein undergoes a reversible P450-to-P420 inactivation with a midpoint at 380 MPa and a reaction volume change of -28 ml/mol. The inactivation transition is retarded, and the absolute reaction volume is decreased by increasing temperature or by mutations that decrease the size of the active site cavity. High pressure affects the tryptophan fluorescence yield, which decreases by about 37% at 480 MPa. The effect is reversible and suggests considerable contraction of the protein. Aerobic decomposition of iron-aryl complexes of the CYP119 T213A mutant under increasing hydrostatic pressure results in variation of the N-arylprotoporphyrin-IX regioisomer (NB:NA:NC:ND) adduct pattern from 39:47:07:07 at 0.1 MPa to 23:36:14:27 at 400 MPa. Preincubation of the protein at 400 MPa followed by complex formation and decomposition give the same regioisomer distribution as untreated protein.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and MonoQ column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, wild-type and mutant enzymes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rabe, K.S.; Kiko, K.; Niemeyer, C.M.
Characterization of the peroxidase activity of CYP119, a thermostable P450 from Sulfolobus acidocaldarius
Chembiochem
9
420-425
2008
Sulfolobus acidocaldarius (Q55080), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (Q55080)
Tschirret-Guth, R.A.; Koo, L.S.; Hoa, G.H.; Ortiz De Montellano, P.R.
Reversible pressure deformation of a thermophilic cytochrome P450 enzyme (CYP119) and its active-site mutants
J. Am. Chem. Soc.
123
3412-3417
2001
Sulfolobus acidocaldarius (Q55080), Sulfolobus acidocaldarius 7 (Q55080)
Koo, L.S.; Tschirret-Guth, R.A.; Straub, W.E.; Monne-Loccoz, P.; Loehr, T.M.; Ortiz de Montellano, P.R.
The active site of the thermophilic CYP119 from Sulfolobus solfataricus
J. Biol. Chem.
275
14112-14123
2000
Sulfolobus acidocaldarius (Q55080), Sulfolobus acidocaldarius DSM 639 (Q55080)
EXTERNAL LINKS (specific for EC-Number 1.11.1.7)
Transporter Classification Database (TCDB): 9.A.61.3.1
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