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Key Documents

06372

Sigma-Aldrich

β-Hydroxypyruvic acid

≥95.0% (dry substance, T)

Synonym(s):

3-Hydroxy-2-oxopropanoic acid

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About This Item

Empirical Formula (Hill Notation):
C3H4O4
CAS Number:
Molecular Weight:
104.06
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32

Assay

≥95.0% (dry substance, T)

form

powder and chunks

impurities

≤15.0% water

storage temp.

2-8°C

SMILES string

OC(C(CO)=O)=O

InChI

1S/C3H4O4/c4-1-2(5)3(6)7/h4H,1H2,(H,6,7)

InChI key

HHDDCCUIIUWNGJ-UHFFFAOYSA-N

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Application


  • Hydroxy(phenyl)pyruvic acid reductase in Actaea racemosa L.: a putative enzyme in cimicifugic and fukinolic acid biosynthesis.: This study investigates the role of ß-Hydroxypyruvic acid in the biosynthesis of bioactive compounds in Actaea racemosa, highlighting its importance in plant secondary metabolism and potential applications in medicinal chemistry (Jahn and Petersen, 2024).

  • The gut microbiota confers protection in the CNS against neurodegeneration induced by manganism.: Research shows the protective role of ß-Hydroxypyruvic acid derivatives produced by gut microbiota against neurodegenerative conditions, providing insights into therapeutic strategies for neurological disorders (Wang et al., 2020).

Biochem/physiol Actions

Metabolite involved in the pathway of carbon in photorespiration.

Pictograms

CorrosionExclamation mark

Signal Word

Danger

Hazard Statements

Hazard Classifications

Acute Tox. 4 Oral - Skin Corr. 1B

Storage Class Code

8A - Combustible corrosive hazardous materials

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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Seong Pil Chung et al.
Journal of biochemistry, 148(6), 743-753 (2010-09-30)
D-amino acid oxidase (DAO) is a flavoenzyme that exists in the kidney, liver and brain of mammals. This enzyme catalyzes the oxidation of D-amino acids to the corresponding α-keto acid, hydrogen peroxide and ammonia. Recently D-serine, one of the substrates
M Legge
Biochimica et biophysica acta, 1355(2), 99-101 (1997-02-04)
Mouse oocytes and zygotes, when solubilised demonstrated that a range of ketoaldehydes could be utilised as substrates. Of the five ketoaldehydes investigated the overall substrate utilisation was hydroxypyruvate > glyoxylate > 2-ketobutyrate > pyruvate > glycolate. The utilisation of these
O A Esakova et al.
IUBMB life, 59(2), 104-109 (2007-04-25)
The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically active holoenzyme (TK* - ThDP).
M C Lawrence et al.
Journal of molecular biology, 266(2), 381-399 (1997-02-21)
We describe here a sub-family of enzymes related both structurally and functionally to N-acetylneuraminate lyase. Two members of this family (N-acetylneuraminate lyase and dihydrodipicolinate synthase) have known three-dimensional structures and we now proceed to show their structural and functional relationship
William E Karsten et al.
Biochimica et biophysica acta, 1790(6), 575-580 (2009-03-07)
The enzyme L-serine-glyoxylate aminotransferase (SGAT) from Hyphomicrobium methylovorum is a PLP-containing enzyme that catalyzes the conversion of L-serine and glyoxylate to hydroxypyruvate and glycine. The cloned enzyme expressed in Escherichia coli is isolated as a mixture of the E:PLP and

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