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Merck
CN

W386901

3-Methyl-2-oxobutanoic acid sodium salt

95%

Synonym(s):

Sodium 3-methyl-2-oxobutyrate, α-Ketoisovaleric acid sodium salt, 2-Keto-3-methylbutyric acid sodium salt, 3-Methyl-2-oxobutanoic acid sodium salt, 3-Methyl-2-oxobutyric acid sodium salt, Ketovaline sodium salt

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About This Item

Linear Formula:
(CH3)2CHCOCOONa
CAS Number:
3715-29-5
Molecular Weight:
138.10
EC Number:
223-062-2
UNSPSC Code:
12164502
PubChem Substance ID:
329830664
Beilstein/REAXYS Number:
4334552
MDL number:
MFCD00002581

Key Documents

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biological source

synthetic

assay

95%

mp

220-230 °C (dec.) (lit.)

application(s)

flavors and fragrances

documentation

see Safety & Documentation for available documents

food allergen

no known allergens

organoleptic

fruity

SMILES string

[Na+].CC(C)C(=O)C([O-])=O

InChI

1S/C5H8O3.Na/c1-3(2)4(6)5(7)8;/h3H,1-2H3,(H,7,8);/q;+1/p-1

InChI key

WIQBZDCJCRFGKA-UHFFFAOYSA-M

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
MKBQ7807V
MKBN6004V
MKBL4850V
MKBH8359V
MKBG0048V

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Felix S Krause et al.
Applied and environmental microbiology, 76(24), 8053-8061 (2010-10-12)
2-Ketoisovalerate is used as a therapeutic agent, and a 2-ketoisovalerate-producing organism may serve as a platform for products deriving from this 2-keto acid. We engineered the wild type of Corynebacterium glutamicum for the growth-decoupled production of 2-ketoisovalerate from glucose by
Marta de la Plaza et al.
Journal of molecular microbiology and biotechnology, 17(2), 96-100 (2008-11-27)
The alpha-ketoisovalerate decarboxylase (Kivd) is a unique lactococcal key enzyme in the decarboxylation of branched-chain alpha-keto acids derived from branched-chain amino acids transamination into aldehydes. These products are important aroma compounds produced during cheese ripening. In this study, the Kivd
Taro Murakami et al.
Journal of nutritional science and vitaminology, 51(1), 48-50 (2005-05-27)
Branched-chain alpha-keto acid dehydrogenase kinase (BDK) phosphorylates and inactivates the branched-chain alpha-keto acid dehydrogenase complex (BCKDC), which is the rate-limiting enzyme in the branched-chain amino acid catabolism. BDK has been believed to be bound to the BCKDC. However, recent our
Benjamin F Miller et al.
The Journal of physiology, 567(Pt 3), 1021-1033 (2005-07-09)
We hypothesized that an acute bout of strenuous, non-damaging exercise would increase rates of protein synthesis of collagen in tendon and skeletal muscle but these would be less than those of muscle myofibrillar and sarcoplasmic proteins. Two groups (n =
Nayden Koon et al.
Proceedings of the National Academy of Sciences of the United States of America, 101(22), 8295-8300 (2004-05-26)
The leucine biosynthetic pathway is essential for the growth of Mycobacterium tuberculosis and is a potential target for the design of new anti-tuberculosis drugs. The crystal structure of alpha-isopropylmalate synthase, which catalyzes the first committed step in this pathway, has
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