06372
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
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32
MDL number:
Assay:
≥95.0% (dry substance, T)
Form:
powder and chunks
InChI key
HHDDCCUIIUWNGJ-UHFFFAOYSA-N
InChI
1S/C3H4O4/c4-1-2(5)3(6)7/h4H,1H2,(H,6,7)
assay
≥95.0% (dry substance, T)
form
powder and chunks
impurities
≤15.0% water
storage temp.
2-8°C
Quality Level
Related Categories
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 β-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 β-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.
signalword
Danger
hcodes
Hazard Classifications
Acute Tox. 4 Oral - Skin Corr. 1B
Storage Class
8A - Combustible corrosive hazardous materials
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Faceshields, Gloves, type P3 (EN 143) respirator cartridges
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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
Juhan Kim et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(42), E2856-E2864 (2012-09-18)
Evolution or engineering of novel metabolic pathways can endow microbes with new abilities to degrade anthropogenic pollutants or synthesize valuable chemicals. Most studies of the evolution of new pathways have focused on the origins and quality of function of the
Chen Yang et al.
Journal of bacteriology, 190(5), 1773-1782 (2007-12-25)
Members of a novel glycerate-2-kinase (GK-II) family were tentatively identified in a broad range of species, including eukaryotes and archaea and many bacteria that lack a canonical enzyme of the GarK (GK-I) family. The recently reported three-dimensional structure of GK-II
Renwick C J Dobson et al.
Protein science : a publication of the Protein Society, 17(12), 2080-2090 (2008-09-13)
In recent years, dihydrodipicolinate synthase (DHDPS, E.C. 4.2.1.52) has received considerable attention from a mechanistic and structural viewpoint. DHDPS catalyzes the reaction of (S)-aspartate-beta-semialdehyde with pyruvate, which is bound via a Schiff base to a conserved active-site lysine (Lys161 in
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
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