Tryptophan 7-halogenase

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Tryptophan 7-halogenase (EC 1.14.19.9, PrnA, RebH) is an enzyme with systematic name L-tryptophan:FADH2 oxidoreductase (7-halogenating).^[1]^[2] This enzyme catalyses the following chemical reaction

tryptophan + FADH₂ + Cl⁻ + O₂ + H⁺

\rightleftharpoons

7-chloro-L-tryptophan + FAD + 2 H₂O

In Lechevalieria aerocolonigenes the enzyme catalyses the initial step in the biosynthesis of rebeccamycin.^[3]

The enzyme can use bromide ions (Br⁻) in place of chloride (Cl⁻).^[4]

References

↑ Dong, C., Kotzsch, A., Dorward, M., van Pee, K.H. and Naismith, J.H. (2004). "Crystallization and X-ray diffraction of a halogenating enzyme, tryptophan 7-halogenase, from Pseudomonas fluorescens". Acta Crystallogr. D Biol. Crystallogr. 60 (Pt 8): 1438–1440. doi:10.1107/S0907444904012521. PMID 15272170.
↑ Dong, C; Flecks, S; Unversucht, S; Haupt, C; Van Pée, K. H.; Naismith, J. H. (2005). "Tryptophan 7-halogenase (PrnA) structure suggests a mechanism for regioselective chlorination". Science 309 (5744): 2216–9. doi:10.1126/science.1116510. PMC 3315827. PMID 16195462.
↑ Bitto, Eduard; Huang, Yu; Bingman, Craig A.; Singh, Shanteri; Thorson, Jon S.; Phillips, George N. (2007). "The structure of flavin-dependent tryptophan 7-halogenase RebH". Proteins: Structure, Function, and Bioinformatics 70 (1): 289–293. doi:10.1002/prot.21627. ISSN 0887-3585. PMID 17876823.
↑ Yeh, E., Garneau, S. and Walsh, C.T. (2005). "Robust in vitro activity of RebF and RebH, a two-component reductase/halogenase, generating 7-chlorotryptophan during rebeccamycin biosynthesis". Proc. Natl. Acad. Sci. USA 102 (11): 3960–3965. doi:10.1073/pnas.0500755102. PMC 554827. PMID 15743914.

External links

Tryptophan 7-halogenase at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)

1.14.11: 2-oxoglutarate	Prolyl hydroxylase Lysyl hydroxylase

1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 Lanosterol 14 alpha-demethylase 24-hydroxycholesterol 7α-hydroxylase

1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1

1.14.15: reduced iron-sulfur protein	11B1 11B2 11A1

1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase

1.14.17: reduced ascorbate	Dopamine beta-hydroxylase

1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1

1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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