X-ray Structures of NADPH-dependent Carbonyl Reductase from Sporobolomyces salmonicolor Provide Insights into Stereoselective Reductions of Carbonyl Compounds

Kamitori, Shigehiro; Iguchi, Akihiro; Ohtaki, Akashi; Yamada, Michihiro; Kita, Keiko

doi:10.1016/j.jmb.2005.07.011

Cited by 58 publications

(55 citation statements)

References 32 publications

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“…The affected regions include the connecting loop b4-a4, a central anchoring element for the bound NADP(H), and a segment that includes two residues of the catalytic triad (Tyr-X-X-X-Lys). The b4-a4 loop is commonly observed in SDRs to be conformationally restricted only in the presence of bound NADPH/substrate (Kamitori et al, 2005). Notably, the amino acid residues involved in interactions with the NADPH cosubstrate are generally highly conserved among all SDR enzymes and in particular within the SDR108E/SDR115E family.…”

Section: Conservation and Dynamics Of Ligand Bindingmentioning

confidence: 99%

Structural Studies of Cinnamoyl-CoA Reductase and Cinnamyl-Alcohol Dehydrogenase, Key Enzymes of Monolignol Biosynthesis

et al. 2014

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The enzymes cinnamoyl-CoA reductase (CCR) and cinnamyl alcohol dehydrogenase (CAD) catalyze the two key reduction reactions in the conversion of cinnamic acid derivatives into monolignol building blocks for lignin polymers in plant cell walls. Here, we describe detailed functional and structural analyses of CCRs from Medicago truncatula and Petunia hybrida and of an atypical CAD (CAD2) from M. truncatula. These enzymes are closely related members of the short-chain dehydrogenase/ reductase (SDR) superfamily. Our structural studies support a reaction mechanism involving a canonical SDR catalytic triad in both CCR and CAD2 and an important role for an auxiliary cysteine unique to CCR. Site-directed mutants of CAD2 (Phe226Ala and Tyr136Phe) that enlarge the phenolic binding site result in a 4-to 10-fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2. This finding demonstrates the potential exploitation of rationally engineered forms of CCR and CAD2 for the targeted modification of monolignol composition in transgenic plants. Thermal denaturation measurements and structural comparisons of various liganded and unliganded forms of CCR and CAD2 highlight substantial conformational flexibility of these SDR enzymes, which plays an important role in the establishment of catalytically productive complexes of the enzymes with their NADPH and phenolic substrates.

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Section: Conservation and Dynamics Of Ligand Bindingmentioning

confidence: 99%

Structural Studies of Cinnamoyl-CoA Reductase and Cinnamyl-Alcohol Dehydrogenase, Key Enzymes of Monolignol Biosynthesis

et al. 2014

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“…In our experiment, we found four transcripts encoding proteins potentially involved in secondary metabolism to be significantly upregulated by resveratrol in the BCR library (Table 3). They encode porphobilinogen synthase (PBGS; BC1G_13189.1/BofuT4_ P104910.1; Jaffe 2004) implicated in the biosynthesis of tetrapyrroles, a putative intradiol dioxygenase implicated in intradiol aromatic ring cleavage (BC1G_13469.1), a NADPHdependent carbonyl reductase (BC1G_06734.1/BofuT4_ P077380.1; Kamitori et al 2005), and an oxidoreductase (BC1G_00711/BofuT4_P020150.1). Thus, it could be suggested that one or several of these transcripts participate in resveratrol metabolism in B. cinerea.…”

Section: Genes Encoding Proteins With Other Rolesmentioning

confidence: 99%

LongSAGE gene-expression profiling of Botrytis cinerea germination suppressed by resveratrol, the major grapevine phytoalexin

et al. 2011

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“…They display different physical and enzymatic properties, show a wide variety of substrate specificities, and are mainly classified into three superfamilies, zinc-dependent alcohol dehydrogenases, short-chain dehydrogenase/reductases (SDRs), and aldo-keto reductases, based on their catalytic properties and sequence information (8,14,32). Among the various enzyme sources, Candida species are attractive as highly stereospecific oxidoreductase donors (4,13,15,16,25,30).…”

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confidence: 99%

Purification, Characterization, Gene Cloning, and Expression of a Novel Alcohol Dehydrogenase with Anti-Prelog Stereospecificity from Candida parapsilosis

Nie

et al. 2007

Appl Environ Microbiol

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An alcohol dehydrogenase from Candida parapsilosis CCTCC M203011 was characterized along with its biochemical activity and structural gene. The amino acid sequence shows similarity to those of the short-chain dehydrogenase/reductases but no overall identity to known proteins. This enzyme with unusual stereospecificity catalyzes an anti-Prelog reduction of 2-hydroxyacetophenone to (S)-1-phenyl-1,2-ethanediol.

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X-ray Structures of NADPH-dependent Carbonyl Reductase from Sporobolomyces salmonicolor Provide Insights into Stereoselective Reductions of Carbonyl Compounds

Cited by 58 publications

References 32 publications

Structural Studies of Cinnamoyl-CoA Reductase and Cinnamyl-Alcohol Dehydrogenase, Key Enzymes of Monolignol Biosynthesis

Structural Studies of Cinnamoyl-CoA Reductase and Cinnamyl-Alcohol Dehydrogenase, Key Enzymes of Monolignol Biosynthesis

LongSAGE gene-expression profiling of Botrytis cinerea germination suppressed by resveratrol, the major grapevine phytoalexin

Purification, Characterization, Gene Cloning, and Expression of a Novel Alcohol Dehydrogenase with Anti-Prelog Stereospecificity from Candida parapsilosis

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