Erratum: Rat Aldose Reductase-Like Protein (AKR1B14) Efficiently Reduces the Lipid Peroxidation Product 4-Oxo-2-nonenal [Biol. Pharm. Bull. 33(11): 1886-1890 (2010)]

Endo, Shunsuke; Matsunaga, Toshiyuki; Fujita, Anna; Tajima, Kazuo; El‐Kabbani, Ossama; Hara, Akira

doi:10.1248/bpb.34.937

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“…However, the two enzymes differ in their K m value for the coenzyme NADP(H). The value for AKR1B14 is lower than that for AKR1B7, which is similar to that for AKR1B1 (Kubiseski & Flynn, 1995;Endo, Matsunaga, Fujita et al, 2010;Endo et al, 2011).…”

Section: Introductionsupporting

confidence: 72%

“…In rats, AKR1B14 has highest amino-acid sequence identity (87%) to the corresponding mouse AR-like protein AKR1B7 (Val et al, 2002). Both AKR1B14 and AKR1B7 show prostaglandin F 2 synthase activity (Lambert-Langlais et al, 2009) and also display broad substrate specificity for various aldehydes, -dicarbonyl compounds and some aromatic ketones (Lefrançois- Martinez et al, 1999;Martinez et al, 2001;Endo, Matsunaga, Fujita et al, 2010). However, the two enzymes differ in their K m value for the coenzyme NADP(H).…”

Section: Introductionmentioning

confidence: 99%

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Structure of the His269Arg mutant of the rat aldose reductase-like protein AKR1B14 complexed with NADPH

et al. 2012

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Rat aldose reductase-like protein (AKR1B14) is an orthologue of mouse vas deferens protein (AKR1B7) and plays roles in the detoxification of reactive aldehydes and synthesis of prostaglandin F 2. Here, the 1.87 Å resolution crystal structure of the His269Arg mutant of AKR1B14 complexed with NADPH is described and shows that the negatively charged 2 0-phosphate group of the coenzyme forms an ionic interaction with the positively charged guanidinium group of Arg269 that is also observed in the human aldose reductase (AKR1B1) structure. Previous experiments on the site-directed mutagenesis of His269 to Arg, Phe and Met revealed fourfold, sevenfold and 127-fold increases in the K m for NADPH, respectively, which are in agreement with the present molecularmodelling and X-ray crystallographic studies. This is the first tertiary structure of a mutant form of this AKR1B7 orthologue to be reported in order to investigate the structure-function relationship of the nonconserved His269 and its role in coenzyme binding.

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Section: Introductionsupporting

confidence: 72%