Beta-carotene 3-hydroxylase

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Beta-carotene 3-hydroxylase
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EC no. 1.14.13.129
CAS no. 133425-64-6
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Beta-carotene 3-hydroxylase (EC 1.14.13.129, beta-carotene 3,3'-monooxygenase, CrtZ) is an enzyme with systematic name beta-carotene,NADH:oxygen 3-oxidoreductase . [1] [2] [3] [4] [5] [6] [7] This enzyme catalyses the following chemical reaction

beta-carotene + 2 NADH + 2 H+ + 2 O2 zeaxanthin + 2 NAD+ + 2 H2O (overall reaction)
(1a) beta-carotene + NADH + H+ + O2 beta-cryptoxanthin + NAD+ + H2O
(1b) beta-cryptoxanthin + NADH + H+ + O2 zeaxanthin + NAD+ + H2O

Beta-carotene 3-hydroxylase requires ferredoxin and Fe(II).

Related Research Articles

<span class="mw-page-title-main">Carotenoid</span> Class of chemical compounds; yellow, orange or red plant pigments

Carotenoids are yellow, orange, and red organic pigments that are produced by plants and algae, as well as several bacteria, archaea, and fungi. Carotenoids give the characteristic color to pumpkins, carrots, parsnips, corn, tomatoes, canaries, flamingos, salmon, lobster, shrimp, and daffodils. Over 1,100 identified carotenoids can be further categorized into two classes – xanthophylls and carotenes.

<span class="mw-page-title-main">Canthaxanthin</span> Chemical compound

Canthaxanthin is a keto-carotenoid pigment widely distributed in nature. Carotenoids belong to a larger class of phytochemicals known as terpenoids. The chemical formula of canthaxanthin is C40H52O2. It was first isolated in edible mushrooms. It has also been found in green algae, bacteria, crustaceans, and bioaccumulates in fish such as carp, golden grey mullet, seabream and trush wrasse.

CRT is the gene cluster responsible for the biosynthesis of carotenoids. Those genes are found in eubacteria, in algae and are cryptic in Streptomyces griseus.

Nitrate reductase (NAD(P)H) (EC 1.7.1.2, assimilatory nitrate reductase, assimilatory NAD(P)H-nitrate reductase, NAD(P)H bispecific nitrate reductase, nitrate reductase (reduced nicotinamide adenine dinucleotide (phosphate)), nitrate reductase NAD(P)H, NAD(P)H-nitrate reductase, nitrate reductase [NAD(P)H2], NAD(P)H2:nitrate oxidoreductase) is an enzyme with systematic name nitrite:NAD(P)+ oxidoreductase. This enzyme catalises the following chemical reaction

Nitrate reductase (NADH) (EC 1.7.1.1, assimilatory nitrate reductase, NADH-nitrate reductase, NADH-dependent nitrate reductase, assimilatory NADH: nitrate reductase, nitrate reductase (NADH2), NADH2:nitrate oxidoreductase) is an enzyme with systematic name nitrite:NAD+ oxidoreductase. This enzyme catalyzes the following chemical reaction

In enzymology, a 7alpha-hydroxysteroid dehydrogenase (EC 1.1.1.159) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3-hydroxybenzoate 6-monooxygenase (EC 1.14.13.24) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3-hydroxyphenylacetate 6-hydroxylase (EC 1.14.13.63) is an enzyme that catalyzes the chemical reaction

In enzymology, a 4-hydroxybenzoate 3-monooxygenase [NAD(P)H] (EC 1.14.13.33) is an enzyme that catalyzes the chemical reaction

In enzymology, a 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase (EC 1.14.13.96) is an enzyme that catalyzes the chemical reaction

In enzymology, a salicylate 1-monooxygenase (EC 1.14.13.1) is an enzyme that catalyzes the chemical reaction

In enzymology, a malonate-semialdehyde dehydrogenase (EC 1.2.1.15) is an enzyme that catalyzes the chemical reaction

Alanine dehydrogenase (EC 1.4.1.1) is an enzyme that catalyzes the chemical reaction

5-exo-hydroxycamphor dehydrogenase (EC 1.1.1.327, F-dehydrogenase, FdeH) is an enzyme with systematic name 5-exo-hydroxycamphor:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction

Pentachlorophenol monooxygenase (EC 1.14.13.50, pentachlorophenol dechlorinase, pentachlorophenol dehalogenase, pentachlorophenol 4-monooxygenase, PCP hydroxylase, pentachlorophenol hydroxylase, PcpB, PCB 4-monooxygenase, PCB4MO) is an enzyme with systematic name pentachlorophenol,NADPH:oxygen oxidoreductase (hydroxylating, dechlorinating). This enzyme catalyses the following chemical reaction

Zeaxanthin epoxidase (EC 1.14.13.90, Zea-epoxidase) is an enzyme with systematic name zeaxanthin,NAD(P)H:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction

Taurochenodeoxycholate 6alpha-hydroxylase (EC 1.14.13.97, CYP3A4, CYP4A21, taurochenodeoxycholate 6alpha-monooxygenase) is an enzyme with systematic name taurochenodeoxycholate,NADPH:oxygen oxidoreductase (6alpha-hydroxylating). This enzyme catalyses the following chemical reaction

3-(3-hydroxyphenyl)propanoate hydroxylase (EC 1.14.13.127, mhpA (gene)) is an enzyme with systematic name 3-(3-hydroxyphenyl)propanoate,NADH:oxygen oxidoreductase (2-hydroxylating). This enzyme catalyses the following chemical reaction

Spheroidene monooxygenase (EC 1.14.15.9, CrtA, acyclic carotenoid 2-ketolase, spirilloxantin monooxygenase, 2-oxo-spirilloxanthin monooxygenase) is an enzyme with systematic name spheroidene, reduced-ferredoxin:oxygen oxidoreductase (spheroiden-2-one-forming). This enzyme catalyses the following chemical reaction

Carotene epsilon-monooxygenase (EC 1.14.99.45, CYP97C1, LUT1) is an enzyme with systematic name alpha-carotene:oxygen oxidoreductase (3-hydroxylating). This enzyme catalyses the following chemical reaction

References

  1. ↑ Sun Z, Gantt E, Cunningham FX (October 1996). "Cloning and functional analysis of the beta-carotene hydroxylase of Arabidopsis thaliana". The Journal of Biological Chemistry. 271 (40): 24349–52. doi: 10.1074/jbc.271.40.24349 . PMID   8798688.
  2. ↑ Fraser PD, Miura Y, Misawa N (March 1997). "In vitro characterization of astaxanthin biosynthetic enzymes". The Journal of Biological Chemistry. 272 (10): 6128–35. doi: 10.1074/jbc.272.10.6128 . PMID   9045623.
  3. ↑ Fraser PD, Shimada H, Misawa N (March 1998). "Enzymic confirmation of reactions involved in routes to astaxanthin formation, elucidated using a direct substrate in vitro assay". European Journal of Biochemistry. 252 (2): 229–36. doi: 10.1046/j.1432-1327.1998.2520229.x . PMID   9523693.
  4. ↑ Bouvier F, Keller Y, d'Harlingue A, Camara B (April 1998). "Xanthophyll biosynthesis: molecular and functional characterization of carotenoid hydroxylases from pepper fruits (Capsicum annuum L.)". Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 1391 (3): 320–8. doi:10.1016/s0005-2760(98)00029-0. PMID   9555077.
  5. ↑ Linden H (September 1999). "Carotenoid hydroxylase from Haematococcus pluvialis: cDNA sequence, regulation and functional complementation". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1446 (3): 203–12. doi:10.1016/s0167-4781(99)00088-3. PMID   10524195.
  6. ↑ Zhu C, Yamamura S, Nishihara M, Koiwa H, Sandmann G (February 2003). "cDNAs for the synthesis of cyclic carotenoids in petals of Gentiana lutea and their regulation during flower development". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1625 (3): 305–8. doi:10.1016/s0167-4781(03)00017-4. PMID   12591618.
  7. ↑ Choi SK, Matsuda S, Hoshino T, Peng X, Misawa N (October 2006). "Characterization of bacterial beta-carotene 3,3'-hydroxylases, CrtZ, and P450 in astaxanthin biosynthetic pathway and adonirubin production by gene combination in Escherichia coli". Applied Microbiology and Biotechnology. 72 (6): 1238–46. doi:10.1007/s00253-006-0426-2. PMID   16614859.
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