EC |
1.6.5.4 |
Accepted name: |
monodehydroascorbate reductase (NADH) |
Reaction: |
NADH + H+ + 2 monodehydroascorbate = NAD+ + 2 ascorbate |
Other name(s): |
NADH:semidehydroascorbic acid oxidoreductase; MDHA; semidehydroascorbate reductase; AFR (ambiguous); AFR-reductase; ascorbic free radical reductase; ascorbate free radical reductase; SOR (ambiguous); MDAsA reductase (NADPH); SDA reductase; NADH:ascorbate radical oxidoreductase; NADH-semidehydroascorbate oxidoreductase; ascorbate free-radical reductase; NADH:AFR oxidoreductase; monodehydroascorbate reductase (NADH2) |
Systematic name: |
NADH:monodehydroascorbate oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-26-9 |
References: |
1. |
Schulze, H.-U., Schott, H.-H. and Staudinger, H. Isolierung und Charakterisierung einer NADH: Semidehydroascorbinsäure-Oxidoreduktase aus Neurospora crassa. Hoppe-Seyler's Z. Physiol. Chem. 353 (1972) 1931–1942. [PMID: 4405497] |
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[EC 1.6.5.4 created 1961] |
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EC
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1.10.2.1
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Deleted entry: | L-ascorbate—cytochrome-b5 reductase. The activity is covered by EC 7.2.1.3, ascorbate ferrireductase (transmembrane) |
[EC 1.10.2.1 created 1972, modified 2000, deleted 2021] |
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EC |
1.10.3.3 |
Accepted name: |
L-ascorbate oxidase |
Reaction: |
4 L-ascorbate + O2 = 4 monodehydroascorbate + 2 H2O |
Other name(s): |
ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate:O2 oxidoreductase; AA oxidase |
Systematic name: |
L-ascorbate:oxygen oxidoreductase |
Comments: |
A multicopper protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-44-1 |
References: |
1. |
Yamazaki, I. and Piette, L.H. Mechanism of free radical formation and disappearance during the ascorbic acid oxidase and peroxidase reactions. Biochim. Biophys. Acta 50 (1961) 62–69. [DOI] [PMID: 13787201] |
2. |
Stark, G.R. and Dawson, C.R. Ascorbic acid oxidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 297–311. |
3. |
Messerschmidt, A., Ladenstein, R., Huber, R., Bolognesi, M., Avigliano, L., Petruzzelli, R., Rossi, A. and Finazzi-Agro, A. Refined crystal structure of ascorbate oxidase at 1.9 Å resolution. J. Mol. Biol. 224 (1992) 179–205. [DOI] [PMID: 1548698] |
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[EC 1.10.3.3 created 1961, modified 2011] |
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EC |
1.11.1.11 |
Accepted name: |
L-ascorbate peroxidase |
Reaction: |
2 L-ascorbate + H2O2 + 2 H+ = L-ascorbate + L-dehydroascorbate + 2 H2O (overall reaction) (1a) 2 L-ascorbate + H2O2 + 2 H+ = 2 monodehydroascorbate + 2 H2O (1b) 2 monodehydroascorbate = L-ascorbate + L-dehydroascorbate (spontaneous) |
Glossary: |
monodehydroascorbate = ascorbate radical |
Other name(s): |
L-ascorbic acid peroxidase; L-ascorbic acid-specific peroxidase; ascorbate peroxidase; ascorbic acid peroxidase |
Systematic name: |
L-ascorbate:hydrogen-peroxide oxidoreductase |
Comments: |
A heme protein. Oxidizes ascorbate and low molecular weight aromatic substrates. The monodehydroascorbate radical produced is either directly reduced back to ascorbate by EC 1.6.5.4 [monodehydroascorbate reductase (NADH)] or undergoes non-enzymic disproportionation to ascorbate and dehydroascorbate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 72906-87-7 |
References: |
1. |
Shigeoka, S., Nakano, Y. and Kitaoka, S. Purification and some properties of L-ascorbic-acid-specific peroxidase in Euglena gracilis. Z. Arch. Biochem. Biophys. 201 (1980) 121–127. [DOI] [PMID: 6772104] |
2. |
Shigeoka, S., Nakano, Y. and Kitaoka, S. Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidase. Biochem. J. 186 (1980) 377–380. [PMID: 6768357] |
3. |
Nakano, Y and Asada, K. Purification of ascorbate peroxidase in spinach chloroplasts; its inactivation in ascorbate-depleted medium and reactivation by monodehydroascorbate radical. Plant Cell Physiol. 28 (1987) 131–140. |
4. |
Patterson, W.R. and Poulos, T.L. Crystal structure of recombinant pea cytosolic ascorbate peroxidase. Biochemistry 34 (1995) 4331–4341. [PMID: 7703247] |
5. |
Sharp, K.H., Moody, P.C., Brown, K.A. and Raven, E.L. Crystal structure of the ascorbate peroxidase-salicylhydroxamic acid complex. Biochemistry 43 (2004) 8644–8651. [DOI] [PMID: 15236572] |
6. |
Macdonald, I.K., Badyal, S.K., Ghamsari, L., Moody, P.C. and Raven, E.L. Interaction of ascorbate peroxidase with substrates: a mechanistic and structural analysis. Biochemistry 45 (2006) 7808–7817. [DOI] [PMID: 16784232] |
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[EC 1.11.1.11 created 1983, modified 2010, modified 2011] |
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EC |
1.14.17.1 |
Accepted name: |
dopamine β-monooxygenase |
Reaction: |
dopamine + 2 ascorbate + O2 = noradrenaline + 2 monodehydroascorbate + H2O |
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For diagram of dopa biosynthesis, click here |
Glossary: |
dopamine = 4-(2-aminoethyl)benzene-1,2-diol |
Other name(s): |
dopamine β-hydroxylase; MDBH (membrane-associated dopamine β-monooxygenase); SDBH (soluble dopamine β-monooxygenase); dopamine-B-hydroxylase; 3,4-dihydroxyphenethylamine β-oxidase; 4-(2-aminoethyl)pyrocatechol β-oxidase; dopa β-hydroxylase; dopamine β-oxidase; dopamine hydroxylase; phenylamine β-hydroxylase; (3,4-dihydroxyphenethylamine)β-mono-oxygenase; DβM (gene name) |
Systematic name: |
dopamine,ascorbate:oxygen oxidoreductase (β-hydroxylating) |
Comments: |
A copper protein. The enzyme, found in animals, binds two copper ions with distinct roles during catalysis. Stimulated by fumarate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-38-1 |
References: |
1. |
Levin, E.Y., Levenberg, B. and Kaufman, S. The enzymatic conversion of 3,4-dihydroxyphenylethylamine to norepinephrine. J. Biol. Chem. 235 (1960) 2080–2086. [PMID: 14416204] |
2. |
Friedman, S. and Kaufman, S. 3,4-Dihydroxyphenylethylamine β-hydroxylase. Physical properties, copper content, and role of copper in the catalytic activity. J. Biol. Chem. 240 (1965) 4763–4773. [PMID: 5846992] |
3. |
Skotland, T. and Ljones, T. Direct spectrophotometric detection of ascorbate free radical formed by dopamine β-monooxygenase and by ascorbate oxidase. Biochim. Biophys. Acta 630 (1980) 30–35. [PMID: 7388045] |
4. |
Evans, J.P., Ahn, K. and Klinman, J.P. Evidence that dioxygen and substrate activation are tightly coupled in dopamine β-monooxygenase. Implications for the reactive oxygen species. J. Biol. Chem. 278 (2003) 49691–49698. [PMID: 12966104] |
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[EC 1.14.17.1 created 1965 as EC 1.14.2.1, transferred 1972 to EC 1.14.17.1, modified 2020] |
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EC |
1.14.17.3 |
Accepted name: |
peptidylglycine monooxygenase |
Reaction: |
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O |
Other name(s): |
peptidylglycine 2-hydroxylase; peptidyl α-amidating enzyme; peptide-α-amide synthetase; peptide α-amidating enzyme; peptide α-amide synthase; peptidylglycine α-hydroxylase; peptidylglycine α-amidating monooxygenase; PAM-A; PAM-B; PAM; peptidylglycine,ascorbate:oxygen oxidoreductase (2-hydroxylating) |
Systematic name: |
[peptide]-glycine,ascorbate:oxygen oxidoreductase (2-hydroxylating) |
Comments: |
A copper protein. The enzyme binds two copper ions with distinct roles during catalysis. Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme. The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalysed by EC 4.3.2.5 peptidylamidoglycolate lyase. In mammals, the two activities are part of a bifunctional protein. Involved in the final step of biosynthesis of α-melanotropin and related biologically active peptides. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 90597-47-0 |
References: |
1. |
Bradbury, A.F., Finnie, M.D.A. and Smyth, D.G. Mechanism of C-terminal amide formation by pituitary enzymes. Nature (Lond.) 298 (1982) 686–688. [PMID: 7099265] |
2. |
Glembotski, C.G. Further characterization of the peptidyl α-amidating enzyme in rat anterior pituitary secretory granules. Arch. Biochem. Biophys. 241 (1985) 673–683. [DOI] [PMID: 2994573] |
3. |
Murthy, A.S.N., Mains, R.E. and Eipper, B.A. Purification and characterization of peptidylglycine α-amidating monooxygenase from bovine neurointermediate pituitary. J. Biol. Chem. 261 (1986) 1815–1822. [PMID: 3944110] |
4. |
Bradbury, A.F. and Smyth, D.G. Enzyme-catalysed peptide amidation. Isolation of a stable intermediate formed by reaction of the amidating enzyme with an imino acid. Eur. J. Biochem. 169 (1987) 579–584. [DOI] [PMID: 3691506] |
5. |
Murthy, A.S.N., Keutmann, H.T. and Eipper, B.A. Further characterization of peptidylglycine α-amidating monooxygenase from bovine neurointermediate pituitary. Mol. Endocrinol. 1 (1987) 290–299. [DOI] [PMID: 3453894] |
6. |
Katopodis, A.G., Ping, D. and May, S.W. A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of α-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine α-amidating monooxygenase in peptide amidation. Biochemistry 29 (1990) 6115–6120. [PMID: 2207061] |
7. |
Prigge, S.T., Kolhekar, A.S., Eipper, B.A., Mains, R.E. and Amzel, L.M. Amidation of bioactive peptides: the structure of peptidylglycine α-hydroxylating monooxygenase. Science 278 (1997) 1300–1305. [PMID: 9360928] |
8. |
Prigge, S.T., Eipper, B.A., Mains, R.E. and Amzel, L.M. Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex. Science 304 (2004) 864–867. [PMID: 15131304] |
9. |
Chufan, E.E., Prigge, S.T., Siebert, X., Eipper, B.A., Mains, R.E. and Amzel, L.M. Differential reactivity between two copper sites in peptidylglycine α-hydroxylating monooxygenase. J. Am. Chem. Soc. 132 (2010) 15565–15572. [PMID: 20958070] |
10. |
Chauhan, S., Hosseinzadeh, P., Lu, Y. and Blackburn, N.J. Stopped-flow studies of the reduction of the copper centers suggest a bifurcated electron transfer pathway in peptidylglycine monooxygenase. Biochemistry 55 (2016) 2008–2021. [PMID: 26982589] |
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[EC 1.14.17.3 created 1989, modified 2019] |
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EC
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1.16.5.1
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Transferred entry: | ascorbate ferrireductase (transmembrane). Now EC 7.2.1.3, ascorbate ferrireductase (transmembrane)
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[EC 1.16.5.1 created 2011, deleted 2018] |
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EC |
7.2.1.3 |
Accepted name: |
ascorbate ferrireductase (transmembrane) |
Reaction: |
ascorbate[side 1] + Fe(III)[side 2] = monodehydroascorbate[side 1] + Fe(II)[side 2] |
Other name(s): |
cytochrome b561 (ambiguous) |
Systematic name: |
Fe(III):ascorbate oxidorectuctase (electron-translocating) |
Comments: |
A diheme cytochrome that transfers electrons across a single membrane, such as the outer membrane of the enterocyte, or the tonoplast membrane of the plant cell vacuole. Acts on hexacyanoferrate(III) and other ferric chelates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Flatmark, T. and Terland, O. Cytochrome b561 of the bovine adrenal chromaffin granules. A high potential b-type cytochrome. Biochim. Biophys. Acta 253 (1971) 487–491. [DOI] [PMID: 4332308] |
2. |
McKie, A.T., Barrow, D., Latunde-Dada, G.O., Rolfs, A., Sager, G., Mudaly, E., Mudaly, M., Richardson, C., Barlow, D., Bomford, A., Peters, T.J., Raja, K.B., Shirali, S., Hediger, M.A., Farzaneh, F. and Simpson, R.J. An iron-regulated ferric reductase associated with the absorption of dietary iron. Science 291 (2001) 1755–1759. [DOI] [PMID: 11230685] |
3. |
Su, D. and Asard, H. Three mammalian cytochromes b561 are ascorbate-dependent ferrireductases. FEBS J. 273 (2006) 3722–3734. [DOI] [PMID: 16911521] |
4. |
Berczi, A., Su, D. and Asard, H. An Arabidopsis cytochrome b561 with trans-membrane ferrireductase capability. FEBS Lett. 581 (2007) 1505–1508. [DOI] [PMID: 17376442] |
5. |
Wyman, S., Simpson, R.J., McKie, A.T. and Sharp, P.A. Dcytb (Cybrd1) functions as both a ferric and a cupric reductase in vitro. FEBS Lett. 582 (2008) 1901–1906. [DOI] [PMID: 18498772] |
6. |
Glanfield, A., McManus, D.P., Smyth, D.J., Lovas, E.M., Loukas, A., Gobert, G.N. and Jones, M.K. A cytochrome b561 with ferric reductase activity from the parasitic blood fluke, Schistosoma japonicum. PLoS Negl. Trop. Dis. 4:e884 (2010). [DOI] [PMID: 21103361] |
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[EC 7.2.1.3 created 2011 as EC 1.16.5.1, transferred 2018 to EC 7.2.1.3] |
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