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Identification
YMDB IDYMDB00900
Nameoxygen
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionOxygen, also known as dioxygene or O2, belongs to the class of inorganic compounds known as other non-metal oxides. These are inorganic compounds containing an oxygen atom of an oxidation state of -2, in which the heaviest atom bonded to the oxygen belongs to the class of 'other non-metals'. Oxygen is possibly neutral. Oxygen exists in all living species, ranging from bacteria to humans.
Structure
Thumb
Synonyms
  • dioxygen
  • dioxygene
  • Disauerstoff
  • molecular oxygen
  • O(2)
  • O2
  • Oxygen
  • Oxygen molecule
  • Pure oxygen
  • [OO]
  • e 948
  • e-948
  • e948
  • Oxygen-16
  • Oxygen 16
CAS number7782-44-7
WeightAverage: 31.9988
Monoisotopic: 31.989829244
InChI KeyMYMOFIZGZYHOMD-UHFFFAOYSA-N
InChIInChI=1S/O2/c1-2
IUPAC Namedioxygen
Traditional IUPAC Namesinglet oxygen
Chemical FormulaO2
SMILESO=O
Chemical Taxonomy
Description belongs to the class of inorganic compounds known as other non-metal oxides. These are inorganic compounds containing an oxygen atom of an oxidation state of -2, in which the heaviest atom bonded to the oxygen belongs to the class of 'other non-metals'.
KingdomInorganic compounds
Super ClassHomogeneous non-metal compounds
ClassOther non-metal organides
Sub ClassOther non-metal oxides
Direct ParentOther non-metal oxides
Alternative Parents
Substituents
  • Other non-metal oxide
  • Inorganic oxide
Molecular FrameworkNot Available
External Descriptors
Physical Properties
StateLiquid
Charge0
Melting point-218.4 °C
Experimental Properties
PropertyValueReference
Water Solubility37.5 mg/mL at 21 oC [VENABLE,CS & FUWA,T (1922)]PhysProp
LogP0.65 [HANSCH,C ET AL. (1995)]PhysProp
Predicted Properties
PropertyValueSource
logP-0.28ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count2ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area34.14 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity2.89 m³·mol⁻¹ChemAxon
Polarizability1.53 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • extracellular
  • mitochondrion
  • endoplasmic reticulum
  • peroxisome
  • cytoplasm
Organoleptic PropertiesNot Available
SMPDB Pathways
Biosynthesis of unsaturated fatty acidsPW002403 ThumbThumb?image type=greyscaleThumb?image type=simple
Biosynthesis of unsaturated fatty acids (docosanoyl)PW002408 ThumbThumb?image type=greyscaleThumb?image type=simple
Biosynthesis of unsaturated fatty acids (icosanoyl)PW002434 ThumbThumb?image type=greyscaleThumb?image type=simple
Biosynthesis of unsaturated fatty acids (stearoyl)PW002435 ThumbThumb?image type=greyscaleThumb?image type=simple
Biosynthesis of unsaturated fatty acids (tetracosanoyl-CoA)PW002404 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Sulfur metabolismec00920 Map00920
Tryptophan metabolismec00380 Map00380
beta-Alanine metabolismec00410 Map00410
SMPDB Reactions
L-Aspartic acid + water + oxygenOxalacetic acid + Ammonia + Hydrogen peroxide
Spermine + water + oxygenHydrogen peroxide + 3-Aminopropionaldehyde + Spermidine
1,2-Dihydroxy-3-keto-5-methylthiopentene + oxygen4-Methylthio-2-oxobutanoate + hydron + Formic acid
hydron + oxygen + ferrocytochrome b5 + Sphinganinewater + Phytosphingosine + ferricytochrome b5
3-Hydroxyanthranilic acid + oxygenhydron + 2-Amino-3-carboxymuconic acid semialdehyde
KEGG Reactions
NADH + ergosta-5,7,24(28)-trien-3beta-ol + hydron + oxygenwater + NAD + ergosta-5,7,22,24(28)-tetraen-3beta-ol
ergosta-5,7,24(28)-trien-3beta-ol + NADPH + hydron + oxygenwater + NADP + ergosta-5,7,22,24(28)-tetraen-3beta-ol
4alpha-methylzymosterol + NADPH + hydron + oxygenNADP + zymosterol intermediate 1a + water
zymosterol intermediate 1a + NADPH + hydron + oxygenwater + zymosterol intermediate 1b + NADP
zymosterol intermediate 1b + NADPH + hydron + oxygenNADP + zymosterol intermediate 1c + water
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyView
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-001i-9000000000-2e78a9ed80eede2ed33aJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-001i-9000000000-a9a93dd42f2cfa0b34c4JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-001i-9000000000-a9a93dd42f2cfa0b34c4JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-001i-9000000000-a9a93dd42f2cfa0b34c4JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-001i-9000000000-5e864878b295db174473JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-001i-9000000000-5e864878b295db174473JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-001i-9000000000-5e864878b295db174473JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-001i-9000000000-9878c3ba827de483e23bJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-001i-9000000000-9878c3ba827de483e23bJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-001i-9000000000-9878c3ba827de483e23bJSpectraViewer
References
References:
  • Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). "BRENDA, the enzyme information system in 2011." Nucleic Acids Res 39:D670-D676.21062828
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Lee, B. H., Huh, W. K., Kim, S. T., Lee, J. S., Kang, S. O. (1999). "Bacterial production of D-erythroascorbic acid and L-ascorbic acid through functional expression of Saccharomyces cerevisiae D-arabinono-1,4-lactone oxidase in Escherichia coli." Appl Environ Microbiol 65:4685-4687.10508108
  • Lepesheva, G. I., Waterman, M. R. (2007). "Sterol 14alpha-demethylase cytochrome P450 (CYP51), a P450 in all biological kingdoms." Biochim Biophys Acta 1770:467-477.16963187
  • Hogan, D. A., Auchtung, T. A., Hausinger, R. P. (1999). "Cloning and characterization of a sulfonate/alpha-ketoglutarate dioxygenase from Saccharomyces cerevisiae." J Bacteriol 181:5876-5879.10482536
  • Marbois, B., Gin, P., Faull, K. F., Poon, W. W., Lee, P. T., Strahan, J., Shepherd, J. N., Clarke, C. F. (2005). "Coq3 and Coq4 define a polypeptide complex in yeast mitochondria for the biosynthesis of coenzyme Q." J Biol Chem 280:20231-20238.15792955
  • Schneiter, R., Tatzer, V., Gogg, G., Leitner, E., Kohlwein, S. D. (2000). "Elo1p-dependent carboxy-terminal elongation of C14:1Delta(9) to C16:1Delta(11) fatty acids in Saccharomyces cerevisiae." J Bacteriol 182:3655-3660.10850979
  • Hiltunen, J. K., Mursula, A. M., Rottensteiner, H., Wierenga, R. K., Kastaniotis, A. J., Gurvitz, A. (2003). "The biochemistry of peroxisomal beta-oxidation in the yeast Saccharomyces cerevisiae." FEMS Microbiol Rev 27:35-64.12697341
  • Geisbrecht, B. V., Zhu, D., Schulz, K., Nau, K., Morrell, J. C., Geraghty, M., Schulz, H., Erdmann, R., Gould, S. J. (1998). "Molecular characterization of Saccharomyces cerevisiae Delta3, Delta2-enoyl-CoA isomerase." J Biol Chem 273:33184-33191.9837886
  • Panozzo, C., Nawara, M., Suski, C., Kucharczyka, R., Skoneczny, M., Becam, A. M., Rytka, J., Herbert, C. J. (2002). "Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae." FEBS Lett 517:97-102.12062417
  • Lamb, D. C., Kelly, D. E., Manning, N. J., Kaderbhai, M. A., Kelly, S. L. (1999). "Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction." FEBS Lett 462:283-288.10622712
  • Kucharczyk, R., Zagulski, M., Rytka, J., Herbert, C. J. (1998). "The yeast gene YJR025c encodes a 3-hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis." FEBS Lett 424:127-130.9539135
  • Kastaniotis, A. J., Autio, K. J., Sormunen, R. T., Hiltunen, J. K. (2004). "Htd2p/Yhr067p is a yeast 3-hydroxyacyl-ACP dehydratase essential for mitochondrial function and morphology." Mol Microbiol 53:1407-1421.15387819
Synthesis Reference:Wynn, Richard L. Production of hydrogen and oxygen by thermal disassociation of water. U.S. Pat. Appl. Publ. (2007), 26pp.
External Links:
ResourceLink
CHEBI ID15379
HMDB IDHMDB01377
Pubchem Compound ID977
Kegg IDC00007
ChemSpider ID952
FOODB IDFDB022589
WikipediaOxygen
BioCyc IDCPD-6641

Enzymes

General function:
Involved in D-arabinono-1,4-lactone oxidase activity
Specific function:
Can oxidize L-gulono-1,4-lactone as well as D-arabinono- 1,4-lactone and L-galactono-1,4-lactone
Gene Name:
ALO1
Uniprot ID:
P54783
Molecular weight:
59493.19922
Reactions
D-arabinono-1,4-lactone + O(2) → dehydro-D-arabinono-1,4-lactone + H(2)O(2).
General function:
Involved in iron ion binding
Specific function:
Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol
Gene Name:
ERG11
Uniprot ID:
P10614
Molecular weight:
60719.80078
Reactions
Obtusifoliol + 3 O(2) + 3 NADPH → 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP(+) + 4 H(2)O.
General function:
Involved in pyridoxamine-phosphate oxidase activity
Specific function:
Catalyzes the oxidation of either pyridoxine 5'- phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP)
Gene Name:
PDX3
Uniprot ID:
P38075
Molecular weight:
26908.0
Reactions
Pyridoxamine 5'-phosphate + H(2)O + O(2) → pyridoxal 5'-phosphate + NH(3) + H(2)O(2).
Pyridoxine 5'-phosphate + O(2) → pyridoxal 5'-phosphate + H(2)O(2).
General function:
Amino acid transport and metabolism
Specific function:
Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance
Gene Name:
FMS1
Uniprot ID:
P50264
Molecular weight:
57805.10156
Reactions
Spermine + O(2) + H(2)O → spermidine + 3-aminopropanal + H(2)O(2).
Spermidine + O(2) + H(2)O → putrescine + 3-aminopropanal + H(2)O(2).
N(1)-acetylspermine + O(2) + H(2)O → spermidine + 3-acetamidopropanal + H(2)O(2).
N(1)-acetylspermidine + O(2) + H(2)O → putrescine + 3-acetamidopropanal + H(2)O(2).
N(8)-acetylspermidine + O(2) + H(2)O → 4-acetamidobutanal + trimethylenediamine + H(2)O(2).
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + H(2)O(2)
Gene Name:
POX1
Uniprot ID:
P13711
Molecular weight:
84041.39844
Reactions
Acyl-CoA + O(2) → trans-2,3-dehydroacyl-CoA + H(2)O(2).
General function:
Involved in fatty acid elongase activity
Specific function:
May be a membrane bound enzyme involved in the highly specific elongation of saturated 14-carbon fatty acids (14:0) to 16-carbon species (16:0)
Gene Name:
ELO1
Uniprot ID:
P39540
Molecular weight:
36233.60156
Reactions
Acyl-CoA + malonyl-CoA → 3-oxoacyl-CoA + CoA + CO(2).
General function:
Involved in acyl carrier activity
Specific function:
Carrier of the growing fatty acid chain in fatty acid biosynthesis. May be involved in the synthesis of very-long-chain fatty acids. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain
Gene Name:
ACP1
Uniprot ID:
P32463
Molecular weight:
13942.5
General function:
Involved in oxygen-dependent protoporphyrinogen oxidase activity
Specific function:
Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX
Gene Name:
HEM14
Uniprot ID:
P40012
Molecular weight:
59702.39844
Reactions
Protoporphyrinogen-IX + 3 O(2) → protoporphyrin-IX + 3 H(2)O(2).
General function:
Involved in coproporphyrinogen oxidase activity
Specific function:
Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III
Gene Name:
HEM13
Uniprot ID:
P11353
Molecular weight:
37711.30078
Reactions
Coproporphyrinogen-III + O(2) + 2 H(+) → protoporphyrinogen-IX + 2 CO(2) + 2 H(2)O.
General function:
Involved in electron carrier activity
Specific function:
Could be a fumarate reductase
Gene Name:
OSM1
Uniprot ID:
P21375
Molecular weight:
55064.80078
Reactions
General function:
Involved in monooxygenase activity
Specific function:
Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid
Gene Name:
BNA4
Uniprot ID:
P38169
Molecular weight:
52428.89844
Reactions
L-kynurenine + NADPH + O(2) → 3-hydroxy-L-kynurenine + NADP(+) + H(2)O.
General function:
Involved in oxidoreductase activity
Specific function:
The outer membrane form may mediate the reduction of outer membrane cytochrome b5, and the soluble inter-membrane space form may transfer electrons from external NADH to cytochrome c, thereby mediating an antimycin-insensitive, energy-coupled oxidation of external NADH by yeast mitochondria. Involved in the reduction of D-erythroascorbyl free radicals
Gene Name:
MCR1
Uniprot ID:
P36060
Molecular weight:
34137.69922
Reactions
NADH + 2 ferricytochrome b5 → NAD(+) + H(+) + 2 ferrocytochrome b5.
General function:
Involved in oxidoreductase activity
Specific function:
Acts as a alpha-ketoglutarate-dependent dioxygenase active on sulfonates. Although taurine is a poor substrate, a variety of other sulfonates are utilized, with the best natural substrates being isethionate and taurocholate
Gene Name:
JLP1
Uniprot ID:
Q12358
Molecular weight:
46982.30078
Reactions
General function:
Involved in heme binding
Specific function:
Required for biosynthesis of nicotinic acid
Gene Name:
BNA2
Uniprot ID:
P47125
Molecular weight:
50774.80078
Reactions
General function:
Involved in protein complex assembly
Specific function:
Required for the assembly of yeast cytochrome oxidase. Involved in the biosynthesis of heme A and the initial step in this pathway, the hydroxylation of heme O, is thought to be catalyzed by a three-component mono-oxygenase consisting of COX15, ferredoxin and ferredoxin reductase
Gene Name:
COX15
Uniprot ID:
P40086
Molecular weight:
54657.89844
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway
Gene Name:
ERG1
Uniprot ID:
P32476
Molecular weight:
55125.39844
Reactions
Squalene + AH(2) + O(2) → (S)-squalene-2,3-epoxide + A + H(2)O.
General function:
Involved in ubiquinone biosynthetic process
Specific function:
Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of COQ3, COQ4, COQ6, COQ7 and COQ9 polypeptides
Gene Name:
COQ4
Uniprot ID:
O13525
Molecular weight:
38626.80078
General function:
Involved in iron ion binding
Specific function:
Catalyzes the first step in the removal of the two C-4 methyl groups of 4,4-dimethylzymosterol
Gene Name:
ERG25
Uniprot ID:
P53045
Molecular weight:
36478.89844
Reactions
4,4-dimethyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O(2) → 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)(+) + H(2)O.
4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O(2) → 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)(+) + 2 H(2)O.
3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)H + O(2) → 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)(+) + H(2)O.
General function:
Involved in ferroxidase activity
Specific function:
Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. Plays a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+). Can store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization. May be involved in regulation of the mitochondrial electron transport chain
Gene Name:
YFH1
Uniprot ID:
Q07540
Molecular weight:
19490.0
Reactions
4 Fe(2+) + 4 H(+) + O(2) → 4 Fe(3+) + 2 H(2)O.
General function:
Involved in 3-hydroxyanthranilate 3,4-dioxygenase activity
Specific function:
Catalyzes the oxidative ring opening of 3- hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate
Gene Name:
BNA1
Uniprot ID:
P47096
Molecular weight:
20234.90039
Reactions
3-hydroxyanthranilate + O(2) → 2-amino-3-carboxymuconate semialdehyde.
General function:
Involved in iron ion binding
Specific function:
Required for hydroxylation of C-4 in the sphingoid moiety of ceramide. Involved in the response to syringomycin
Gene Name:
SUR2
Uniprot ID:
P38992
Molecular weight:
40734.0
Reactions
General function:
Involved in metal ion binding
Specific function:
Destroys radicals which are normally produced within the cells and which are toxic to biological systems
Gene Name:
SOD1
Uniprot ID:
P00445
Molecular weight:
15854.59961
Reactions
2 superoxide + 2 H(+) → O(2) + H(2)O(2).
General function:
Involved in superoxide dismutase activity
Specific function:
Destroys radicals which are normally produced within the cells and which are toxic to biological systems
Gene Name:
SOD2
Uniprot ID:
P00447
Molecular weight:
25774.09961
Reactions
2 superoxide + 2 H(+) → O(2) + H(2)O(2).
General function:
Involved in catalytic activity
Specific function:
In the de novo pyrimidine biosynthesic pathway, catalyzes the stereospecific oxidation of (S)-dihydroorotate to orotate and the reduction of fumarate to succinate. Does not use oxaloacetate and NAD or NADP as electron acceptors
Gene Name:
URA1
Uniprot ID:
P28272
Molecular weight:
34800.60156
Reactions
(S)-dihydroorotate + O(2) → orotate + H(2)O(2).
(S)-dihydroorotate + a quinone → orotate + a quinol
General function:
Involved in oxidoreductase activity
Specific function:
This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5
Gene Name:
NCP1
Uniprot ID:
P16603
Molecular weight:
76771.10156
Reactions
NADPH + n oxidized hemoprotein → NADP(+) + n reduced hemoprotein.
General function:
Involved in iron ion binding
Specific function:
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain
Gene Name:
CYC1
Uniprot ID:
P00044
Molecular weight:
12181.90039
Reactions
General function:
Involved in iron ion binding
Specific function:
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain
Gene Name:
CYC7
Uniprot ID:
P00045
Molecular weight:
12532.2998
Reactions
General function:
Involved in stearoyl-CoA 9-desaturase activity
Specific function:
Utilizes O(2) and electrons from the reduced cytochrome b(5) domain to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates (Probable)
Gene Name:
OLE1
Uniprot ID:
P21147
Molecular weight:
58402.60156
Reactions
Stearoyl-CoA + 2 ferrocytochrome b5 + O(2) + 2 H(+) → oleoyl-CoA + 2 ferricytochrome b5 + 2 H(2)O.
General function:
Involved in heme binding
Specific function:
Ceramide hydroxylase involved in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids. Hydroxylates the very long chain fatty acid of ceramides at C2 and C3
Gene Name:
SCS7
Uniprot ID:
Q03529
Molecular weight:
44881.10156
Reactions
General function:
Involved in iron ion binding
Specific function:
Catalyzes the introduction of a C-5 double bond in the B ring of ergosterol. May contribute to the regulation of ergosterol biosynthesis
Gene Name:
ERG3
Uniprot ID:
P32353
Molecular weight:
42729.89844
Reactions
General function:
Involved in catalase activity
Specific function:
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide
Gene Name:
CTT1
Uniprot ID:
P06115
Molecular weight:
64583.0
Reactions
2 H(2)O(2) → O(2) + 2 H(2)O.
General function:
Involved in catalase activity
Specific function:
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide
Gene Name:
CTA1
Uniprot ID:
P15202
Molecular weight:
58555.19922
Reactions
2 H(2)O(2) → O(2) + 2 H(2)O.
General function:
Involved in thiol oxidase activity
Specific function:
FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation in the endoplasmic reticulum lumen in parallel to ERO1
Gene Name:
ERV2
Uniprot ID:
Q12284
Molecular weight:
22141.30078
Reactions
4 R'C(R)SH + O(2) → 2 R'C(R)S-S(R)CR' + 2 H(2)O.
General function:
Involved in thiol oxidase activity
Specific function:
FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS). Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine residues in MIA40 in an oxidized state. Reduced ERV1 is reoxidized by cytochrome c. Required for the maturation of cytoplasmic, but not of mitochondrial Fe/S proteins
Gene Name:
ERV1
Uniprot ID:
P27882
Molecular weight:
21639.30078
Reactions
4 R'C(R)SH + O(2) → 2 R'C(R)S-S(R)CR' + 2 H(2)O.
General function:
Involved in oxidoreductase activity
Specific function:
Electron donor reductase for cytochrome b5. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes. Plays a role in bud morphology
Gene Name:
CBR1
Uniprot ID:
P38626
Molecular weight:
31493.59961
Reactions
NADH + 2 ferricytochrome b5 → NAD(+) + H(+) + 2 ferrocytochrome b5.