KEGG ENZYME: 1.14.19.82

ENZYME: 1.14.19.82

Entry

EC 1.14.19.82               Enzyme

Name

tryptophan 5-brominase (NADPH);
sktB (gene name);
aetF (gene name)

Class

Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water

Sysname

L-tryptophan:NADPH oxidoreductase (5-brominating)

Reaction(IUBMB)

L-tryptophan + NADPH + bromide + O2 + H+ = 5-bromo-L-tryptophan + NADP+ + 2 H2O [RN:R13631]

Reaction(KEGG)

R13631

Substrate

L-tryptophan [CPD:C00078];
NADPH [CPD:C00005];
bromide [CPD:C01324];
O2 [CPD:C00007];
H+ [CPD:C00080]

Product

5-bromo-L-tryptophan [CPD:C23128];
NADP+ [CPD:C00006];
H2O [CPD:C00001]

Comment

Contains FAD. The enzyme was isolated from the cyanobacteria Nostoc punctiforme and Aetokthonos hydrillicola. Unlike most other described tryptophan halogenases, the enzyme is self-sufficient and does not require a flavin reductase (single component halogenase). The enzyme from Aetokthonos hydrillicola also catalyses a second bromination reaction at the 7 position. cf. EC 1.14.19.58, tryptophan 5-halogenase.

History

EC 1.14.19.82 created 2025

Orthology

K28723

tryptophan 5-brominase (NADPH)

K28724

tryptophan 5-brominase (NADPH)

Genes

NCW:	NIES2107_04390

NOSU:

JYQ62_15350

HBQ:	QI031_11935

RIV:	Riv7116_1662

Reference

1 [PMID:33766860]

Authors

Breinlinger S, Phillips TJ, Haram BN, Mares J, Martinez Yerena JA, Hrouzek P, Sobotka R, Henderson WM, Schmieder P, Williams SM, Lauderdale JD, Wilde HD, Gerrin W, Kust A, Washington JW, Wagner C, Geier B, Liebeke M, Enke H, Niedermeyer THJ, Wilde SB.

Title

Hunting the eagle killer: A cyanobacterial neurotoxin causes vacuolar myelinopathy.

Journal

Science 371:371/6536/eaax9050 (2021)
DOI:10.1126/science.aax9050

Sequence

[ag:QNL15176]

Reference

2 [PMID:35142504]

Authors

Adak S, Lukowski AL, Schafer RJB, Moore BS.

Title

From Tryptophan to Toxin: Nature's Convergent Biosynthetic Strategy to Aetokthonotoxin.