Anthranilate 1,2-dioxygenase

Chang H-K, P Mohsen, GJ Zylstra (2003) Characterization and regulation of the genes for a novel anthranilate 1,2-dioxygenase from Burkholderia cepacia DBOl. J Bacterial 185 5871-5881. 

Eby DM, ZM Beharry, ED Coulter, DM Kurtz, EL Neidle (2001) Characterization and evolution of anthranilate 1,2-dioxygenase from Acmetohacfer sp. strain ADPl./Sacfeno/ 183 109-118. 

ANTHOCYANIDIN SYNTHASE ANTHRANILATE 1,2-DIOXYGENASE ANTHRANILATE HYDROXYLASE... 

The dioxygenase nature of these reactions was first demonstrated by Kobayashi et al.201 with anthranilate 1,2-dioxygenase (hydroxylase). They demonstrated by experiments with 180 that both atoms of oxygen in catechol are exclusively derived from molecular oxygen. Subsequently, the incorporation of two atoms of molecular oxygen into substrates was established by tracer experiments with benzene 1,2-dioxygenase204 and benzoate 1,2-dioxygenase206. ... 

O. 14 g/L. Another new artificial biosynthetic route has been described for E. coli that uses besides glucose also glycerol as substrate. Anthranilic acid, the first intermediate in the blocked tryptophan biosynthetic branch, was subsequently converted to catechol and di,c -muconic acid (Sun et al., 2013). Genes for anthranilate 1,2-dioxygenase and catechol 1,2-dioxygenase were coexpressed fromP. aeruginosa and... 

An enzymatic pathway for indole degradation was found in A. niger, inducible by the substrate within a 5-h period during growth. Among the enzymes found, anthranilate hydroxylase, N-formylanthranilate deformylase, 2,3-dihydroxybenzoate decarboxylase, and catechol dioxygenase were isolated, and their activities were demonstrated in a cell-free system [342],... 

Decarbonilyzing (CO removal) enzyme 1H-3-OH-4-oxoQN-2, 4-dioxygenase BDN through the anthranilic acid pathway ... 

This enzyme [EC 1.14.13.35], also referred to as anthranilate 3-monooxygenase (deaminating) and anthranilate 2,3-dioxygenase (a transferred entry, formerly EC 1.14.12.2), catalyzes the reaction of anthranilate with NADPH and dioxygen to generate 2,3-dihydroxybenzo-... 

ADENYLYLSULFATE REDUCTASE ANTHRANILATE L,2-DIOXYGENASE BENZENE L,2-DIOXYGENASE BENZOATE L,2-DIOXYGENASE CARBON MONOXIDE DEHYDROGENASE... 

Returning to the major tryptophan catabolic pathway, marked by green arrows in Fig. 25-11, formate is removed hydrolytically (step c) from the product of tryptophan dioxygenase action to form kynurenine, a compound that is acted upon by a number of enzymes. Kynureninase (Eq. 14-35) cleaves the compound to anthranilate and alanine (step d), while transamination leads to the cyclic kynurenic acid (step e). Hie latter is dehydroxylated in an unusual reaction to quinaldic acid, a prominent urinary excretion product. 

The degradation of quinol-4-one involves initial hydroxylation at C3 but ring cleavage is then mediated by a dioxygenase with the formation of anthranilate (Block and Lingens 1992). 

Similar reactions were reported for the broad-substrate-specific benzoate dioxygenase of Rhodococcus sp. strain 19070[2G. Recombinant E. coli containing this enzyme transform benzoate and anthranilate to catechol and 2-hydro-l,2-dihydroxybenzoate, respectively. 

Indirect evidence for the existence of such an enzyme arose from the observation [30] that in vitro administration of anthranilic acid to rat neurons causes an increase in intracellular HA concentration. However, that study did not pay due attention to the earlier observation [31], that anthranilic acid is an effective inhibitor (Ki 40 pM) of the enzyme, devoted to HA oxidation, 3-hydroxyanthranilate oxidase (dioxygenase). Therefore, the increase in HA concentration could well be due to an inhibitory effect of anthranilic acid towards the further catabolism of HA, and not to a direct conversion of anthranilic acid to HA. 

Samples of (3R)- and (3S)-[3- Hi]tryptophans 331 have been converted to the corresponding kynurenines 336 using the enzymes tryptophan dioxygenase (EC 1.13.11.11) and formylkynurenine formamidase (EC 3.5.1.9). These have been used to investigate the fission of kynurenine 336 to anthranilic acid 300 and alanine 337 in H20 (337) (Scheme 85). Conversion of the alanine to acetate and assessment of sense of chirality indicated that... 

Hydroxyanthranilate dioxygenase (E.C. 1.13.11.6 - 3-Hydroxy-anthranilate oxygen 3,4-oxidoreductase (decyclizing)... 

All known dioxygenases contain iron, either in heme groups or as Fe-S centers. Some also contain copper. Examples are 1Vyptophan-2,3-dioxygenase (see), homogentisate oxidase (see L-Phenylalanine), 3-hydroxy-anthranilate oxidase (see L-llyptophan). 

Degradation of L-tryptophan in most organisms proceeds via L-kynurenine, 3-hydroxy-L-kynurenine, 3-hydroxyanthranilic acid and quinolinic acid to acetyl Co A and CO2 (Fig. 244). Anthranilic acid formed as an intermediate may be recycled to L-tryptophan (see above). The ring of 3-hydroxyanthranilic acid is cleaved by a dioxygenase (C 2.5). The x-amino-/3-carboxymuconic acid-e-semialdehyde formed either undergoes a cis trans isomerization of the Zl -double bond and cyclization to quinolinic acid, a compound synthesized in microorganisms and plants from aspartic acid and D-glyceraldehyde-3-phosphate (D 16.2). On the other hand o -amino-/3-carboxymuconic acid-e-aldehyde may be de-carboxylated and is then the immediate precursor of NH3, acetic acid and COg. 

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