Protein Family Models

This domain is found in Enoyl-(Acyl carrier protein) reductases. (from Pfam)

Date:

2024-08-14

This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group [1]. [1]. 23790488. Structural and stereochemical analysis of a modular polyketide. synthase ketoreductase domain required for the generation of a. cis-alkene.. Bonnett SA, Whicher JR, Papireddy K, Florova G, Smith JL,. Reynolds KA;. Chem Biol. 2013;20:772-783. (from Pfam)

Date:

2024-08-14

This family contains a wide variety of dehydrogenases. [1]. 9735295. The refined crystal structure of Drosophila lebanonensis alcohol. dehydrogenase at 1.9 A resolution.. Benach J, Atrian S, Gonzalez-Duarte R, Ladenstein R;. J Mol Biol 1998;282:383-399.. [2]. 10387002. Structure of tropinone reductase-II complexed with NADP+ and. pseudotropine at 1.9 A resolution: implication for. stereospecific substrate binding and catalysis.. Yamashita A, Kato H, Wakatsuki S, Tomizaki T, Nakatsu T,. Nakajima K, Hashimoto T, Yamada Y, Oda J;. Biochemistry 1999;38:7630-7637. (from Pfam)

Date:

2024-08-14

gluconate 5-dehydrogenase catalyzes the reversible NADP-dependent oxidation of gluconate to 5-ketogluconate

Date:

2019-07-29

Involved in the nonphosphorylative, ketogenic oxidation of glucose and oxidizes gluconate to 5-ketogluconate

Date:

2021-10-18

The dhuD gene in Streptococcus agalactiae NEM316 is located in the UGL cluster, which contains genes involved in heparin and hyaluronan degradation. DhuD is involved in 4-deoxy-L-threo-hex-4-enopyranuronate degradation. The primary structure of DhuD is significantly different from that of KduD enzyme, which catalyze the same reaction, suggesting their parallel evolution.

Gene:

dhuD

Date:

2019-03-15