918-44-5

Usage

Uses

Used in Sports Nutrition:
2-Hydroxy-2-methyl-3-oxobutanoic acid is used as a nutritional supplement for enhancing muscle synthesis and maintenance. It supports the body's ability to build and preserve muscle tissue, which is particularly beneficial for athletes and individuals engaged in regular physical activity.
Used in Exercise Physiology:
In the field of exercise physiology, 2-Hydroxy-2-methyl-3-oxobutanoic acid is utilized to improve athletic performance and recovery. Its role in energy production and muscle maintenance contributes to enhanced physical endurance and reduced muscle fatigue.
Used in Medical Research and Drug Development:
2-Hydroxy-2-methyl-3-oxobutanoic acid is employed as a subject of medical research for its potential antioxidant and anti-inflammatory properties. These characteristics make it a promising candidate for the development of therapeutic agents targeting various health conditions and diseases.
Used in Metabolic Studies:
In the scientific community, 2-Hydroxy-2-methyl-3-oxobutanoic acid is used as a research tool in metabolic studies, particularly focusing on the understanding of leucine metabolism and its implications in energy production and muscle health.

InChI:InChI=1/C5H8O4/c1-3(6)5(2,9)4(7)8/h9H,1-2H3,(H,7,8)

Upstream product

• 25409-39-6 (±)-ethyl 2-acetoxy-2-methylacetoacetate 
• 849585-22-4 LACTIC ACID 
• 75-36-5 acetyl chloride 
• 127-17-3 2-oxo-propionic acid 
• 113-24-6 sodium pyruvate 
• 2706-75-4 sodium glyoxylate 
• 609-14-3 2-acetylpropanoic acid ethyl ester 
• 935-92-2 2,3,5-Trimethyl-1,4-benzoquinone 
• 64-19-7 acetic acid 

Downstream Products

• 513-86-0 3-hydroxy-2-butanon 
• 53584-56-8 (R)-acetoin 
• 431-03-8 dimethylglyoxal 
• 2861-48-5 butane-2,3-dione-bis-phenylhydrazone 

Relevant academic research and scientific papers

Improving the acidic stability of Staphylococcus aureus α-acetolactate decarboxylase in Bacillus subtilis by changing basic residues to acidic residues

The α-acetolactate decarboxylase (ALDC) can reduce diacetyl fleetly to promote mature beer. A safe strain Bacillus subtilis WB600 for high-yield production of ALDC was constructed with the ALDC gene saald from Staphylococcus aureus L3-15. SDS-PAGE analysis revealed that S. aureus α-acetolactate decarboxylase (SaALDC) was successfully expressed in recombinant B. siutilis strain. The enzyme SaALDC was purified using Ni-affinity chromatography and showed a maximum activity at 45 °C and pH 6.0. The values of K m and V max were 17.7 μM and 2.06 mM min-1, respectively. Due to the unstable property of SaALDC at low pH conditions that needed in brewing process, site-directed mutagenesis was proposed for improving the acidic stability of SaALDC. Homology comparative modeling analysis showed that the mutation (K52D) gave rise to the negative-electrostatic potential on the surface of protein while the numbers of hydrogen bonds between the mutation site (N43D) and the around residues increased. Taken together the effect of mutation N43D-K52D, recombinant SaALDCN43D-K52D showed dramatically improved acidic stability with prolonged half-life of 3.5 h (compared to the WT of 1.5 h) at pH 4.0. In a 5-L fermenter, the recombinant B. subtilis strain that could over-express SaALDCN43D-K52D exhibited a high yield of 135.8 U mL-1 of SaALDC activity, about 320 times higher comparing to 0.42 U mL-1 of S. aureus L3-15. This work proposed a strategy for improving the acidic stability of SaALDC in the B. subtilis host.

ENZYMATIC METHODS FOR ISOBUTANOL PRODUCTION

The present invention relates to a process of producing isobutanol, including: mixing water, lactate, an enzyme mixture including at least one enzyme, at least one cofactor, and at least one coenzyme, to prepare a reaction mixture; allowing catalytic conversions of lactate in the reaction mixture for a sufficient amount of time to produce isobutanol; and separating the isobutanol from a reactant obtained by the catalytic conversions, in which the conversion of lactate into isobutanol is in association with a NAD+/NADH and/or NADP+/NADPH regenerating system.

An artificial enzymatic reaction cascade for a cell-free bio-system based on glycerol

Conversion of glycerol into high-value products is of significant importance for sustainability in the biofuel industry. In this study, pyruvic acid, a central intermediate needed for the production of versatile biomolecules, was produced from glycerol without the addition of any cofactors by the cell-free bio-system composed of alditol oxidase, dihydroxy acid dehydratase, and catalase. (3R)-Acetoin was then produced at 85.5% of the theoretical yield from glycerol by α-acetolactate synthase and α-acetolactate decarboxylase. Since other biomolecules can also be produced from pyruvic acid, the cell-free bio-system might serve as a versatile bio-production platform, and support the viability of the biofuel economy. This journal is

Glyoxylate carboligase: A unique thiamin diphosphate-dependent enzyme that can cycle between the 4′-aminopyrimidinium and 1′,4′- iminopyrimidine tautomeric forms in the absence of the conserved glutamate

Glyoxylate carboligase (GCL) is a thiamin diphosphate (ThDP)-dependent enzyme, which catalyzes the decarboxylation of glyoxylate and ligation to a second molecule of glyoxylate to form tartronate semialdehyde (TSA). This enzyme is unique among ThDP enzyme

REACTION OF 1,2,4-TRIMETHYLBENZENE WITH PERACETIC ACID

The oxidation of 1,2,4-trimethylbenzene with peracetic acid leads to the formation of trimethylphenols and hydroquinones, which undergo transformations to the corresponding benzoquinones and products from oxidative cleavage of the ring.The controlling stage of the process is the electrophilic hydroxylation of 1,2,4-trimethylbenzene.

Hydrocortisone esters, pharmaceutical formulations containing these and processes for their preparation

Hydrocortisone esters of the formula STR1 wherein R1 is H, formyl or acetyl and R2 is H or CH3 are antiphlogistically active.