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线性分子式:
(CH3)2CHCOCOONa
化学文摘社编号:
分子量:
138.10
UNSPSC Code:
12352100
NACRES:
NA.22
PubChem Substance ID:
EC Number:
223-062-2
Beilstein/REAXYS Number:
4334552
MDL number:
Assay:
95%
Form:
solid
InChI key
WIQBZDCJCRFGKA-UHFFFAOYSA-M
InChI
1S/C5H8O3.Na/c1-3(2)4(6)5(7)8;/h3H,1-2H3,(H,7,8);/q;+1/p-1
SMILES string
[Na+].CC(C)C(=O)C([O-])=O
assay
95%
form
solid
greener alternative product score
old score: 14
new score: 9
Find out more about DOZN™ Scoring
greener alternative product characteristics
Waste Prevention
Atom Economy
Safer Solvents and Auxiliaries
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sustainability
Greener Alternative Product
mp
220-230 °C (dec.) (lit.)
solubility
water: soluble 100 mg/mL, clear, colorless
functional group
ketone
greener alternative category
Quality Level
Application
3-甲基-2-氧代丁酸钠(3-甲基-2-氧代丁酸钠盐)用于合成 (S)-2-羟基-3-甲基丁酸 。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
An evaluation of the substrate specificity and asymmetric synthesis potential of the cloned L-lactate dehydrogenase from Bacillus stearothermophilus.
Canadian Journal of Chemistry, 67(6), 1065-1070 (1989)
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
Frances H A Huisman et al.
Biochemistry, 51(11), 2289-2297 (2012-02-23)
α-Isopropylmalate synthase (α-IPMS) catalyzes the metal-dependent aldol reaction between α-ketoisovalerate (α-KIV) and acetyl-coenzyme A (AcCoA) to give α-isopropylmalate (α-IPM). This reaction is the first committed step in the biosynthesis of leucine in bacteria. α-IPMS is homodimeric, with monomers consisting of
Joachim Schuster et al.
Plant molecular biology, 57(2), 241-254 (2005-04-12)
Plants are capable to de novo synthesize the essential amino acids leucine, isoleucine and valine. Studies in recent years, however, also revealed that plants have the potential to degrade leucine or may be all of the branched-chain amino acids. One
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