41453-55-8

Basic information

• Product Name: 4-hydroxy-2-oxopentanoic acid
• CAS NO: 41453-55-8
• Molecular Weight: 132.116
• Mol File: 41453-55-8.mol
• Article Data: 4

Chemical Properties

• CAS DataBase Reference: 4-hydroxy-2-oxopentanoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: 4-hydroxy-2-oxopentanoic acid(41453-55-8)
• EPA Substance Registry System: 4-hydroxy-2-oxopentanoic acid(41453-55-8)

Safety Data

• Hazardous Substances Data: 41453-55-8(Hazardous Substances Data)

Upstream product

• 127-17-3 2-oxo-propionic acid 
• 20406-62-6 2-oxopent-4-enoic acid 
• 783334-77-0 2-hydroxymuconic 6-semialdehyde 
• 3685-55-0 2-hydroxymuconic acid 
• 113-24-6 sodium pyruvate 
• 75-07-0 acetaldehyde 
• 1944-45-2 4-methyl-2-oxobutyrolactone 

Downstream Products

• 626-99-3 1,3-butadiene-1-carboxylic acid 
• 107-89-1 acetaldol 
• 20406-62-6 2-oxopent-4-enoic acid 
• 67951-43-3 2-hydroxypent-4-enoic acid 
• 81357-28-0 (RS)-3-hydroxy-4-pentenoic acid 
• 328-42-7 Oxalacetic acid 

Relevant articles and documents

MICROORGANISMS FOR PRODUCING 4C-5C COMPOUNDS WITH UNSATURATION AND METHODS RELATED THERETO

The invention provides a non-naturally occurring microbial organism having a butadiene, crotyl alcohol, 2,4-pentadienoate, 3-buten-2-ol, or 3-buten-1-ol, pathway. The microbial organism contains at least one exogenous nucleic acid encoding an enzyme in a pathway. The invention additionally provides a method for producing butadiene, crotyl alcohol, 2,4-pentadienoate, 3-buten-2-ol, or 3-buten-1-ol,. The method can include culturing a butadiene, crotyl alcohol, 2,4-pentadienoate, 3-buten-2-ol, or 3-buten-1-ol-producing microbial organism, where the microbial organism expresses at least one exogenous nucleic acid encoding a pathway enzyme in a sufficient amount, and under conditions and for a sufficient period of time to produce butadiene, crotyl alcohol, 2,4-pentadienoate, 3-buten-2-ol, or 3-buten-1-ol.

Probing the molecular basis of substrate specificity, stereospecificity, and catalysis in the class II pyruvate aldolase, BphI

BphI, a pyruvate-specific class II aldolase found in the polychlorinated biphenyls (PCBs) degradation pathway, catalyzes the reversible C-C bond cleavage of (4S)-hydroxy-2-oxoacids to form pyruvate and an aldehyde. Mutations were introduced into bphI to probe the contribution of active site residues to substrate recognition and catalysis. In contrast to the wild-type enzyme that has similar specificities for acetaldehyde and propionaldehyde, the L87A variant exhibited a 40-fold preference for propionaldehyde over acetaldehyde. The specificity constant of the L89A variant in the aldol addition reaction using pentaldehyde is increased ～50-fold, making it more catalytically efficient for pentaldehyde utilization compared to the wild-type utilization of the natural substrate, acetaldehyde. Replacement of Tyr-290 with phenylalanine or serine resulted in a loss of stereochemical control as the variants were able to utilize substrates with both R and S configurations at C4 with similar kinetic parameters. Aldol cleavage and pyruvate α-proton exchange activity were undetectable in the R16A variant, supporting the role of Arg-16 in stabilizing a pyruvate enolate intermediate. The pH dependence of the enzyme is consistent with a single deprotonation by a catalytic base with pKa values of approximately 7. In H20A and H20S variants, pH profiles show the dependence of enzyme activity on hydroxide concentration. On the basis of these results, a catalytic mechanism is proposed.