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Literature summary for 1.3.1.3 extracted from

  • Di Costanzo, L.; Penning, T.M.; Christianson, D.W.
    Aldo-keto reductases in which the conserved catalytic histidine is substituted (2009), Chem. Biol. Interact., 178, 127-133.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structure of the 5beta-POR-NADP+ binary complex reveals that 5beta-POR exhibits a characteristic short-chain dehydrogenase fold with an N-terminal domain consisting of a double Rossmann fold for cofactor binding and an insertional domain between strands betaF and betaG of about 100 residues for substrate binding, crystal structure of the 5beta-POR-NADP+ binary complex reveals that the side chain of K147 is found in a similar position to the lysine residue of the YXX(S)K motif in standard short-chain dehydrogenases Digitalis lanata

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Digitalis lanata AKR1D1 catalyzes the stereospecific reduction of the delta4-double-bond of circulating steroid hormones that contain the delta4-3-ketosteroid functionality, e.g. the reduction of testosteron, progesterone and cortisol to yield the corresponding 5-dihydrosteroid ?
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?
additional information Digitalis lanata aldo-keto reductases are a major superfamily of monomeric NADPH-dependent carbonyl oxidoreductases, active site contains conserved residues D50, Y55, K84, and H117 ?
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?
additional information Digitalis lanata the steroid 5beta-reductases catalyze a reaction that is unique in steroid enzymology since the resultant product contains a cis-A/B ring configuration and accordingly contains a 90° bend, the cis-A/B ring configuration is an essential characteristic of cardiac glycosides, e.g. digioxin and bile acids and their precursors ?
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?
progesterone + NADPH + H+ Digitalis lanata stereospecific reduction of the 4-double-bond in cardenolide biosynthesis 5beta-pregnane-3,20-dione + NADP+
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?

Organism

Organism UniProt Comment Textmining
Digitalis lanata
-
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information AKR1D1 catalyzes the stereospecific reduction of the delta4-double-bond of circulating steroid hormones that contain the delta4-3-ketosteroid functionality, e.g. the reduction of testosteron, progesterone and cortisol to yield the corresponding 5-dihydrosteroid Digitalis lanata ?
-
?
additional information aldo-keto reductases are a major superfamily of monomeric NADPH-dependent carbonyl oxidoreductases, active site contains conserved residues D50, Y55, K84, and H117 Digitalis lanata ?
-
?
additional information the steroid 5beta-reductases catalyze a reaction that is unique in steroid enzymology since the resultant product contains a cis-A/B ring configuration and accordingly contains a 90° bend, the cis-A/B ring configuration is an essential characteristic of cardiac glycosides, e.g. digioxin and bile acids and their precursors Digitalis lanata ?
-
?
progesterone + NADPH + H+ stereospecific reduction of the 4-double-bond in cardenolide biosynthesis Digitalis lanata 5beta-pregnane-3,20-dione + NADP+
-
?

Synonyms

Synonyms Comment Organism
5beta-POR
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Digitalis lanata
AKR1D1
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Digitalis lanata
aldo-keto reductase
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Digitalis lanata
steroid 5beta-reductase
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Digitalis lanata

Cofactor

Cofactor Comment Organism Structure
NAD(P)H
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Digitalis lanata