Katana VentraIP

Aldo-keto reductase

The aldo-keto reductase family is a family of proteins that are subdivided into 16 categories; these include a number of related monomeric NADPH-dependent oxidoreductases, such as aldehyde reductase, aldose reductase, prostaglandin F synthase, xylose reductase, rho crystallin, and many others.[1]

Aldo/keto reductase family

Aldo_ket_red

1a80​, 1abn​, 1ads​, 1ae4​, 1afs​, 1ah0​, 1ah3​, 1ah4​, 1az1​, 1az2​, 1c9w​, 1cwn​, 1dla​, 1ef3​, 1eko​, 1el3​, 1exb​, 1frb​, 1gve​, 1hqt​, 1hw6​, 1iei​, 1ihi​, 1j96​, 1jez​, 1k8c​, 1lqa​, 1lwi​, 1m9h​, 1mar​, 1mi3​, 1mrq​, 1mzr​, 1og6​, 1pwl​, 1pwm​, 1pyf​, 1pz0​, 1pz1​, 1q13​, 1q5m​, 1qrq​, 1qwk​, 1r38​, 1ral​, 1ry0​, 1ry8​, 1s1p​, 1s1r​, 1s2a​, 1s2c​, 1sm9​, 1t40​, 1t41​, 1ur3​, 1us0​, 1vbj​, 1vp5​, 1x96​, 1x97​, 1x98​, 1xf0​, 1xgd​, 1xjb​, 1ye4​, 1ye6​, 1z3n​, 1z89​, 1z8a​, 1z9a​, 1zgd​, 1zq5​, 1zsx​, 2a79​, 2acq​, 2acr​, 2acs​, 2acu​, 2agt​, 2alr​, 2bgq​, 2bgs​, 2bp1​, 2c91​, 2clp​, 2dux​, 2duz​, 2dv0​, 2f2k​, 2f38​, 2fgb​, 2fvl​, 2fz8​, 2fz9​, 2fzb​, 2fzd​, 2hdj​, 2he5​, 2he8​, 2hej​, 2hv5​, 2hvn​, 2hvo​, 2i16​, 2i17​, 2ikg​, 2ikh​, 2iki​, 2ikj​, 2ine​, 2inz​, 2ipf​, 2ipg​, 2ipj​, 2ipw​, 2iq0​, 2iqd​, 2is7​, 2isf​, 2j8t​, 2nvc​, 2nvd​, 2p5n​, 2pd5​, 2pd9​, 2pdb​, 2pdc​, 2pdf​, 2pdg​, 2pdh​, 2pdi​, 2pdj​, 2pdk​, 2pdl​, 2pdm​, 2pdn​, 2pdp​, 2pdq​, 2pdu​, 2pdw​, 2pdx​, 2pdy​, 2pev​, 2pf8​, 2pfh​, 2pzn​, 2qxw​, 2r9r​, 2vdg​, 3bcj​, 3bur​, 3buv​, 3bv7​, 3c3u​, 3cmf​, 3cot​, 3eau

Structure[edit]

All possess a similar structure, with a beta-alpha-beta fold characteristic of nucleotide binding proteins.[2] The fold comprises a parallel beta-8/alpha-8-barrel, which contains a novel NADP-binding motif. The binding site is located in a large, deep, elliptical pocket in the C-terminal end of the beta sheet, the substrate being bound in an extended conformation. The hydrophobic nature of the pocket favours aromatic and apolar substrates over highly polar ones.[3]


Binding of the NADPH coenzyme causes a massive conformational change, reorienting a loop, effectively locking the coenzyme in place. This binding is more similar to FAD- than to NAD(P)-binding oxidoreductases.[4]

Examples[edit]

Some proteins of this family contain a potassium channel beta chain regulatory domain; these are reported to have oxidoreductase activity.[5]

AKR1

Steroidogenic enzyme