91817-50-4

Basic information

• Product Name: 2-Pentanone, 1-hydroxy-1-phenyl-, (R)-
• CAS NO: 91817-50-4
• Molecular Formula: C11H14O2
• Molecular Weight: 178.231
• Mol File: 91817-50-4.mol

Chemical Properties

• CAS DataBase Reference: 2-Pentanone, 1-hydroxy-1-phenyl-, (R)-(CAS DataBase Reference)
• NIST Chemistry Reference: 2-Pentanone, 1-hydroxy-1-phenyl-, (R)-(91817-50-4)
• EPA Substance Registry System: 2-Pentanone, 1-hydroxy-1-phenyl-, (R)-(91817-50-4)

Safety Data

• Hazardous Substances Data: 91817-50-4(Hazardous Substances Data)

Upstream product

• 4358-86-5 (2R)-mandelamide 
• 927-77-5 n-propylmagnesium bromide 
• 91877-81-5 (E)-(S)-1-Hydroxy-1-phenyl-pent-3-en-2-one 
• 100-52-7 benzaldehyde 
• 1821-02-9 2-oxopentanoic acid 
• 123-72-8 butyraldehyde 
• 13022-83-8 2-oxopentanoic acid sodium salt 
• 91817-47-9 (E)-(S)-4-(2-Methoxy-ethoxymethoxy)-2-methylsulfanyl-1-phenyl-pent-2-en-1-ol 

Downstream Products

• 91817-51-5 (R)-((4R,5R)-4,5-Dimethyl-2-propyl-[1,3]dioxolan-2-yl)-phenyl-methanol 
• 91817-51-5 (S)-((4R,5R)-4,5-Dimethyl-2-propyl-[1,3]dioxolan-2-yl)-phenyl-methanol 

Relevant articles and documents

Unifying Scheme for the Biosynthesis of Acyl-Branched Sugars: Extended Substrate Scope of Thiamine-Dependent Enzymes

Thiamine diphosphate (ThDP) dependent enzymes are useful catalysts for asymmetric C?C bond formation through benzoin-type condensation reactions that result in α-hydroxy ketones. A wide range of aldehydes and ketones can be used as acceptor substrates; however, the donor substrate range is mostly limited to achiral α-keto acids and simple aldehydes. By using a unifying retro-biosynthetic approach towards acyl-branched sugars, we identified a subclass of (myco)bacterial ThDP-dependent enzymes with a greatly extended donor substrate range, namely functionalized chiral α-keto acids with a chain length from C4 to C8. Highly enantioenriched acyloin products were obtained in good to high yields and several reactions were performed on a preparative scale. The newly introduced functionalized α-keto acids, accessible by known aldolase-catalyzed transformations, substantially broaden the donor substrate range of ThDP-dependent enzymes, thus enabling a more general use of these already valuable catalysts.

Branched-chain keto acid decarboxylase from Lactococcus lactis (KdcA), a valuable thiamine diphosphate-dependent enzyme for asymmetric C - C bond formation

The thiamine diphosphate-dependent, branched-chain 2-keto acid decarboxylase from Lactococcus lactis sup. cremoris Bl157 (KdcA) is a new valuable enzyme for the synthesis of chiral 2-hydroxy ketones. The gene was cloned and the enzyme was expressed as an

Decarboxylative Incorporation of α-Oxobutyrate and α-Oxovalerate into (R)-α-Hydroxyethyl- and n-Propyl Ketones on Reaction with Aromatic and α,β-Unsaturated Aldehydes in Baker's Yeast

Decarboxylative incorporation of linear C3, C4, and C5 α-oxo acids into (R) α-hydroxy ketones (2), (9) and (10) is observed when benzaldehyde (1) is incubated with baker's yeast; α,β-unsaturated aldehydes (11) and (15) with the C3 and C4 acids yield (R)-α