The Enzyme Database

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EC 1.13.11.65     
Accepted name: carotenoid isomerooxygenase
Reaction: zeaxanthin + O2 = (3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal
For diagram of zeaxanthin biosynthesis, click here
Other name(s): ninaB (gene name)
Systematic name: zeaxanthin:oxygen 15,15′-oxidoreductase (bond-cleaving, cis-isomerizing)
Comments: The enzyme, characterized from the moth Galleria mellonella and the fruit fly Drosophila melanogaster, is involved in the synthesis of retinal from dietary caroteoids in insects. The enzyme accepts different all-trans carotenoids, including β-carotene, α-carotene and lutein, and catalyses the symmetrical cleavage of the carotenoid and the simultaneous isomerization of only one of the products to a cis configuration. When the substrate is hydroxylated only in one side (as in cryptoxanthin), the enzyme preferentially isomerizes the hydroxylated part of the molecule.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Oberhauser, V., Voolstra, O., Bangert, A., von Lintig, J. and Vogt, K. NinaB combines carotenoid oxygenase and retinoid isomerase activity in a single polypeptide. Proc. Natl. Acad. Sci. USA 105 (2008) 19000–19005. [DOI] [PMID: 19020100]
[EC 1.13.11.65 created 2012 as EC 1.14.13.164, transferred 2012 to EC 1.13.11.65]
 
 
EC 1.14.13.90      
Transferred entry: zeaxanthin epoxidase. Now EC 1.14.15.21, zeaxanthin epoxidase
[EC 1.14.13.90 created 2005, deleted 2016]
 
 
EC 1.14.13.129      
Transferred entry: β-carotene 3-hydroxylase. Now EC 1.14.15.24, β-carotene 3-hydroxylase.
[EC 1.14.13.129 created 2011, deleted 2017]
 
 
EC 1.14.13.164      
Transferred entry: carotenoid isomerooxygenase. The enzyme was discovered at the public-review stage to have been misclassified and so was withdrawn. See EC 1.13.11.65, carotenoid isomerooxygenase
[EC 1.14.13.164 created 2012, deleted 2012]
 
 
EC 1.14.14.158     
Accepted name: carotenoid ε hydroxylase
Reaction: (1) α-carotene + [reduced NADPH-hemoprotein reductase] + O2 = α-cryptoxanthin + [oxidized NADPH-hemoprotein reductase] + H2O
(2) zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2 = lutein + [oxidized NADPH-hemoprotein reductase] + H2O
For diagram of lutein biosynthesis, click here
Other name(s): CYP97C1; LUT1; CYP97C; carotene ε-monooxygenase
Systematic name: α-carotene,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Pogson, B., McDonald, K.A., Truong, M., Britton, G. and DellaPenna, D. Arabidopsis carotenoid mutants demonstrate that lutein is not essential for photosynthesis in higher plants. Plant Cell 8 (1996) 1627–1639. [DOI] [PMID: 8837513]
2.  Tian, L., Musetti, V., Kim, J., Magallanes-Lundback, M. and DellaPenna, D. The Arabidopsis LUT1 locus encodes a member of the cytochrome P450 family that is required for carotenoid ε-ring hydroxylation activity. Proc. Natl. Acad. Sci. USA 101 (2004) 402–407. [DOI] [PMID: 14709673]
3.  Stigliani, A.L., Giorio, G. and D'Ambrosio, C. Characterization of P450 carotenoid β- and ε-hydroxylases of tomato and transcriptional regulation of xanthophyll biosynthesis in root, leaf, petal and fruit. Plant Cell Physiol. 52 (2011) 851–865. [PMID: 21450689]
4.  Chang, S., Berman, J., Sheng, Y., Wang, Y., Capell, T., Shi, L., Ni, X., Sandmann, G., Christou, P. and Zhu, C. Cloning and functional characterization of the maize (Zea mays L.) carotenoid ε hydroxylase gene. PLoS One 10:e0128758 (2015). [PMID: 26030746]
5.  Reddy, C.S., Lee, S.H., Yoon, J.S., Kim, J.K., Lee, S.W., Hur, M., Koo, S.C., Meilan, J., Lee, W.M., Jang, J.K., Hur, Y., Park, S.U. and Kim, A.YB. Molecular cloning and characterization of carotenoid pathway genes and carotenoid content in Ixeris dentata var. albiflora. Molecules 22 (2017) . [DOI] [PMID: 28858245]
[EC 1.14.14.158 created 2011 as EC 1.14.99.45, transferred 2018 to EC 1.14.14.158]
 
 
EC 1.14.15.21     
Accepted name: zeaxanthin epoxidase
Reaction: zeaxanthin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + 2 O2 = violaxanthin + 4 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O (overall reaction)
(1a) zeaxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = antheraxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1b) antheraxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = violaxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
For diagram of the xanthophyll cycle, click here
Other name(s): Zea-epoxidase
Systematic name: zeaxanthin,reduced ferredoxin:oxygen oxidoreductase
Comments: A flavoprotein (FAD) that is active under conditions of low light. Along with EC 1.23.5.1, violaxanthin de-epoxidase, this enzyme forms part of the xanthophyll (or violaxanthin) cycle, which is involved in protecting the plant against damage by excess light. It will also epoxidize lutein in some higher-plant species.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 149718-34-3
References:
1.  Buch, K., Stransky, H. and Hager, A. FAD is a further essential cofactor of the NAD(P)H and O2-dependent zeaxanthin-epoxidase. FEBS Lett. 376 (1995) 45–48. [DOI] [PMID: 8521963]
2.  Bugos, R.C., Hieber, A.D. and Yamamoto, H.Y. Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants. J. Biol. Chem. 273 (1998) 15321–15324. [DOI] [PMID: 9624110]
3.  Thompson, A.J., Jackson, A.C., Parker, R.A., Morpeth, D.R., Burbidge, A. and Taylor, I.B. Abscisic acid biosynthesis in tomato: regulation of zeaxanthin epoxidase and 9-cis-epoxycarotenoid dioxygenase mRNAs by light/dark cycles, water stress and abscisic acid. Plant Mol. Biol. 42 (2000) 833–845. [PMID: 10890531]
4.  Hieber, A.D., Bugos, R.C. and Yamamoto, H.Y. Plant lipocalins: violaxanthin de-epoxidase and zeaxanthin epoxidase. Biochim. Biophys. Acta 1482 (2000) 84–91. [DOI] [PMID: 11058750]
5.  Frommolt, R., Goss, R. and Wilhelm, C. The de-epoxidase and epoxidase reactions of Mantoniella squamata (Prasinophyceae) exhibit different substrate-specific reaction kinetics compared to spinach. Planta 213 (2001) 446–456. [PMID: 11506368]
6.  Frommolt, R., Goss, R. and Wilhelm, C. Erratum Report. The de-epoxidase and epoxidase reactions of Mantoniella squamata (Prasinophyceae) exhibit different substrate-specific reaction kinetics compared to spinach. Planta 213 (2001) 492.
7.  Matsubara, S., Morosinotto, T., Bassi, R., Christian, A.L., Fischer-Schliebs, E., Luttge, U., Orthen, B., Franco, A.C., Scarano, F.R., Forster, B., Pogson, B.J. and Osmond, C.B. Occurrence of the lutein-epoxide cycle in mistletoes of the Loranthaceae and Viscaceae. Planta 217 (2003) 868–879. [DOI] [PMID: 12844265]
[EC 1.14.15.21 created 2005 as EC 1.14.13.90, transferred 2016 to EC 1.14.15.21]
 
 
EC 1.14.15.24     
Accepted name: β-carotene 3-hydroxylase
Reaction: β-carotene + 4 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + 2 O2 = zeaxanthin + 4 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O (overall reaction)
(1a) β-carotene + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 = β-cryptoxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1b) β-cryptoxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 = zeaxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
For diagram of lutein biosynthesis, click here and for diagram of zeaxanthin biosynthesis, click here
Other name(s): β-carotene 3,3′-monooxygenase; CrtZ
Systematic name: β-carotene,reduced ferredoxin [iron-sulfur] cluster:oxygen 3-oxidoreductase
Comments: Requires ferredoxin and iron(II). Also acts on other carotenoids with a β-end group. In some species canthaxanthin is the preferred substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sun, Z., Gantt, E. and Cunningham, F.X., Jr. Cloning and functional analysis of the β-carotene hydroxylase of Arabidopsis thaliana. J. Biol. Chem. 271 (1996) 24349–24352. [DOI] [PMID: 8798688]
2.  Fraser, P.D., Miura, Y. and Misawa, N. In vitro characterization of astaxanthin biosynthetic enzymes. J. Biol. Chem. 272 (1997) 6128–6135. [DOI] [PMID: 9045623]
3.  Fraser, P.D., Shimada, H. and Misawa, N. Enzymic confirmation of reactions involved in routes to astaxanthin formation, elucidated using a direct substrate in vitro assay. Eur. J. Biochem. 252 (1998) 229–236. [DOI] [PMID: 9523693]
4.  Bouvier, F., Keller, Y., d'Harlingue, A. and Camara, B. Xanthophyll biosynthesis: molecular and functional characterization of carotenoid hydroxylases from pepper fruits (Capsicum annuum L.). Biochim. Biophys. Acta 1391 (1998) 320–328. [DOI] [PMID: 9555077]
5.  Linden, H. Carotenoid hydroxylase from Haematococcus pluvialis: cDNA sequence, regulation and functional complementation. Biochim. Biophys. Acta 1446 (1999) 203–212. [DOI] [PMID: 10524195]
6.  Zhu, C., Yamamura, S., Nishihara, M., Koiwa, H. and Sandmann, G. cDNAs for the synthesis of cyclic carotenoids in petals of Gentiana lutea and their regulation during flower development. Biochim. Biophys. Acta 1625 (2003) 305–308. [DOI] [PMID: 12591618]
7.  Choi, S.K., Matsuda, S., Hoshino, T., Peng, X. and Misawa, N. Characterization of bacterial β-carotene 3,3′-hydroxylases, CrtZ, and P450 in astaxanthin biosynthetic pathway and adonirubin production by gene combination in Escherichia coli. Appl. Microbiol. Biotechnol. 72 (2006) 1238–1246. [DOI] [PMID: 16614859]
[EC 1.14.15.24 created 2011 as EC 1.14.13.129, transferred 2017 to EC 1.14.15.24]
 
 
EC 1.14.99.45      
Transferred entry: carotene ε-monooxygenase. Now EC 1.14.14.158, carotene ε-monooxygenase
[EC 1.14.99.45 created 2011, deleted 2018]
 
 
EC 3.4.19.6     
Accepted name: pyroglutamyl-peptidase II
Reaction: Release of the N-terminal pyroglutamyl group from pGlu┼His-Xaa tripeptides and pGlu┼His-Xaa-Gly tetrapeptides
Other name(s): thyroliberinase; pyroglutamyl aminopeptidase II; thyrotropin-releasing factor pyroglutamate aminopeptidase; pyroglutamate aminopeptidase II; pyroglutamyl peptidase II; thyroliberin-hydrolyzing pyroglutamate aminopeptidase; thyrotropin-releasing hormone-degrading pyroglutamate aminopeptidase; thyrotropin-releasing hormone-degrading peptidase; TRH aminopeptidase
Comments: Highly specific for thyrotropin releasing hormone (pyroglutamyl-histidyl-prolylamide). Will not cleave the pyroglutamyl-histidyl bond of luteinizing hormone releasing hormone. Found in serum and brain. Inhibited by metal chelators. In peptidase family M1 (membrane alanyl aminopeptidase family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 60063-88-9
References:
1.  Bauer, K. and Nowak, P. Characterization of a thyroliberin-degrading serum enzyme catalyzing the hydrolysis of thyroliberin at the pyroglutamyl-histidine bond. Eur. J. Biochem. 99 (1979) 239–246. [DOI] [PMID: 115687]
2.  O'Connor, B. and O'Cuinn, G. Purification of and kinetic studies on a narrow specifity synaptosomal membrane pyroglutamate aminopeptidase from guinea-pig brain. Eur. J. Biochem. 150 (1985) 47–52. [DOI] [PMID: 2862039]
3.  Wilk, S. and Wilk, E.K. Pyroglutamyl peptidase II, a thyrotropin releasing hormone degrading enzyme: purification and specificity studies of the rabbit brain enzyme. Neurochem. Int. 15 (1989) 81–89. [PMID: 20504468]
[EC 3.4.19.6 created 1992]
 
 
EC 3.4.21.93     
Accepted name: proprotein convertase 1
Reaction: Release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg┼ bonds
Other name(s): prohormone convertase 3; neuroendocrine convertase 1; PC1
Comments: A Ca2+-dependent enzyme, maximally active at about pH 5.5. Substrates include pro-opiomelanocortin, prorenin, proenkephalin, prodynorphin, prosomatostatin and proinsulin. Unlike prohormone convertase 2, does not hydrolyse proluteinizing-hormone-releasing-hormone. Unusually, processing of prodynorphin occurs at a bond in which P2 is Thr. Present in the regulated secretory pathway of neuroendocrine cells, commonly acting co-operatively with prohormone convertase 2. In peptidase family S8 (subtilisin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 99676-46-7
References:
1.  Seidah, N.G., Gaspar, L., Mion, P., Marcinkiewicz, M., Mbikay, M. and Chrétien, M. cDNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases. DNA Cell Biol. 9 (1990) 415–424. [DOI] [PMID: 2169760]
2.  Smeekens, S.P., Avruch, A.S., LaMendola, J., Chan, S.J. and Steiner, D.F. Identification of a cDNA encoding a second putative prohormone convertase related to PC2 in AtT20 cells and islets of Langerhans. Proc. Natl. Acad. Sci. USA 88 (1991) 340–344. [DOI] [PMID: 1988934]
3.  Steiner, D.F., Smeekens, S.P., Ohagi, S. and Chan, S.J. The new enzymology of precursor processing endoproteases. J. Biol. Chem. 267 (1992) 23435–23438. [PMID: 1429684]
4.  Seidah, N.G. and Chrétien, M. Pro-protein convertases of the subtilisin/kexin family. Methods Enzymol. 244 (1994) 175–188. [DOI] [PMID: 7845206]
5.  Jean, F., Basak, A., Dimaio, J., Seidah, N.G. and Lazure, C. An internally quenched fluorogenic substrate of prohormone convertase 1 and furin leads to a potent prohormone convertase inhibitor. Biochem. J. 307 (1995) 689–695. [PMID: 7741698]
[EC 3.4.21.93 created 1996]
 
 
EC 3.4.21.94     
Accepted name: proprotein convertase 2
Reaction: Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg┼ bonds
Other name(s): neuroendocrine convertase 2; PC2
Comments: A Ca2+-dependent enzyme, maximally active at about pH 5.5. Specificity is broader than that of prohormone convertase 1. Substrates include pro-opiomelanocortin, proenkephalin, prodynorphin, proglucagon, proinsulin and proluteinizing-hormone-releasing-hormone. Does not hydrolyse prorenin or prosomatostatin, however. Unusually, processing of prodynorphin occurs at a bond in which P2 is Thr. Present in the regulated secretory pathway of neuroendocrine cells, commonly acting co-operatively with prohormone convertase 1. In peptidase family S8 (subtilisin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 388092-42-0
References:
1.  Seidah, N.G., Gaspar, L., Mion, P., Marcinkiewicz, M., Mbikay, M. and Chrétien, M. cDNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases. DNA Cell Biol. 9 (1990) 415–424. [DOI] [PMID: 2169760]
2.  Smeekens, S.P. and Steiner, D.F. Identification of a human insulinoma cDNA encoding a novel mammalian protein structurally related to the yeast dibasic processing protease Kex2. J. Biol. Chem. 265 (1990) 2997–3000. [PMID: 2154467]
3.  Rouillé, Y., Westermark, G., Martin, S.K. and Steiner, D.F. Proglucagon is processed to glucagon by prohormone convertase PC2 in alphaTC1-6 cells. Proc. Natl. Acad. Sci. USA 91 (1994) 3242–3246. [DOI] [PMID: 8159732]
4.  Seidah, N.G. and Chrétien, M. Pro-protein convertases of the subtilisin/kexin family. Methods Enzymol. 244 (1994) 175–188. [DOI] [PMID: 7845206]
[EC 3.4.21.94 created 1996]
 
 
EC 5.3.3.22     
Accepted name: lutein isomerase
Reaction: lutein = meso-zeaxanthin
For diagram of lutein biosynthesis, click here
Glossary: lutein = (3R,3′R)-dihydroxy-α-carotene
meso-zeaxanthin = (3R,3′S)-β,β-carotene-3,3′-diol
Other name(s): RPE65 (gene name); meso-zeaxanthin isomerase
Systematic name: lutein Δ45-isomerase
Comments: The enzyme is found in the retinal pigment epithelium (RPE) of vertebrates. It also has the activity of EC 3.1.1.64, retinoid isomerohydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Shyam, R., Gorusupudi, A., Nelson, K., Horvath, M.P. and Bernstein, P.S. RPE65 has an additional function as the lutein to meso-zeaxanthin isomerase in the vertebrate eye. Proc. Natl. Acad. Sci. USA 114 (2017) 10882–10887. [DOI] [PMID: 28874556]
[EC 5.3.3.22 created 2018]
 
 


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