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Aldo-keto reductase

Aldo/keto reductase with broad substrate spectrum. Catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols. Highest enzymatic efficiency is observed with 4-oxonon-2-enal (4-ONE) and 4-hydroxynon-2-enal (4-HNE), that are lipid peroxidation products, and 9,10-phenanthrenequinone (9,10-PQ), a photoproduct of phenanthrene that is one of the most prevalent polycyclic aromatic hydrocarbons in the environment. Is also active on sugar-derived reactive carbonyls such as methylglyoxal (MG), glyoxal and 3-deoxyglucosone (3-DG), and on other lipid-derived carbonyls such as acrolein. May be involved in the detoxification of the toxic lipid peroxidation products 4-ONE and 4-HNE besides many other exo- and endogenic reactive carbonyl compounds (RCs) that may lead to photoinhibition or other cell damages.

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Aldo/keto reductase slr0942

Also known as Aldo/keto reductase slr0942 (AKR) (AKR3G1).
Aldo/keto reductase with broad substrate spectrum. Catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols. Highest enzymatic efficiency is observed with 4-oxonon-2-enal (4-ONE) and 4-hydroxynon-2-enal (4-HNE), that are lipid peroxidation products, and 9,10-phenanthrenequinone (9,10-PQ), a photoproduct of phenanthrene that is one of the most prevalent polycyclic aromatic hydrocarbons in the environment. Is also active on sugar-derived reactive carbonyls such as methylglyoxal (MG), glyoxal and 3-deoxyglucosone (3-DG), and on other lipid-derived carbonyls such as acrolein. May be involved in the detoxification of the toxic lipid peroxidation products 4-ONE and 4-HNE besides many other exo- and endogenic reactive carbonyl compounds (RCs) that may lead to photoinhibition or other cell damages.

Aldo-keto reductase AKR2E4

Also known as Aldo-keto reductase AKR2E4 (3-dehydroecdysone reductase) (Aldo-keto reductase 2E).
NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. May play a role in the regulation of molting. Has lower activity with phenylglyoxal and isatin (in vitro). Has no activity with NADH as cosubstrate. Has no activity with nitrobenzaldehyde and 3-hydroxybenzaldehyde.

Aldo-keto reductase ausK

Also known as Aldo-keto reductase ausK (Austinol synthesis protein K).
Aldo-keto reductase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). AusK also produces the shunt product (5'R)-isoaustinone using preaustinoid A4 as substrate (PubMed:22329759).

Aldo-keto reductase dtxS3

Also known as Aldo-keto reductase dtxS3 (Destruxin synthesis protein 3).
Aldo-keto reductase; part of the gene cluster that mediates the biosynthesis of destruxins, insecticidal cyclic hexadepsipeptides which induce flaccid paralysis and visceral muscle contraction in insects through targeting the calcium channels and vacuolar-type ATPases (PubMed:22232661). The aldo-keto reductase dtxS3 converts alpha-ketoisocaproic acid from deaminated leucine into alpha-hydroxyisocaproic acid (HIC), which is the first substrate for destruxin assembly by dtxS1 (PubMed:22232661). L-aspartate decarboxylase dtxS4 converts aspartic acid into beta-alanine, the last substrate for the destruxin assembly line performed by dtxS1 (PubMed:22232661). The nonribosomal peptide synthetase dtxS1 synthesizes destruxins B and B2, whereas the cytochrome P450 monooxygenase dtxS2 is required to convert destruxin B into other destruxin derivatives, including destructins C, D, A and E (PubMed:22232661). Destruxin E-diol (ED) is further produced in a non-enzymatic manner from destruxin E (PubMed:22232661). Destruxins play an important role in virulence and escape from insect host immune defenses (PubMed:22232661).
Proteins Root Name Listing
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