• Product NameValine
  • CasNo. 7004-03-7
  • MFC5H11NO2
  • MW117.14600
  • Purity
  • Appearance
  • Packing
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Product Details

CasNo: 7004-03-7

MF: C5H11NO2

Buy High Grade Best Quality Valine 7004-03-7 Efficient Delivery

  • Molecular Formula:C5H11NO2
  • Molecular Weight:117.14600
  • Melting Point:315oC 
  • PSA:63.32000 
  • LogP:0.75460 
  • IDLH:1426 
  • IDLH:3444 

Valine(Cas 7004-03-7) Usage

Description

Valine is an essential α-amino acid that plays a vital role in protein biosynthesis. Structurally, it contains an α-amino group, an α-carboxylic acid group, and a side chain comprised of an isopropyl group, which renders it a non-polar aliphatic amino acid.

Uses

Valine is integral to the process of protein synthesis, where it serves as one of the building blocks for the construction of proteins. During translation, ribosomes utilize messenger RNA (mRNA) templates to assemble amino acids, including valine, into polypeptide chains according to the genetic code. Branched-chain amino acids, including valine, are utilized by the body as substrates for energy production. During periods of increased energy demand, such as exercise or metabolic stress, valine can be oxidized in skeletal muscle to generate ATP, the primary energy currency of the cell.

Synthesis

Valine can be synthesized by hydrolysis of aminoisobutyronitrile which is obtained by amination and cyanation of aminoisoaldehyde.

Who Evaluation

Evaluation year: 2004

InChI:InChI:1S/C5H11NO2/c1-3(2)4(6)5(7)8/h3-4H,6H2,1-2H3,(H,7,8)

7004-03-7 Relevant articles

Polyketides, diketopiperazines and an isochromanone from the marine-derived fungal strain Fusarium graminearum FM1010 from Hawaii

Cao, Shugeng,Sarotti, Ariel M.,Uz Zaman, KH Ahammad,Wu, Xiaohua

, (2022/03/09)

The fungal strain Fusarium graminearum F...

Enlarging the Amino Acid Set of Escherichia coli by Infiltration of the Valine Coding Pathway

VOLKER DÖRING, HENNING D. MOOTZ, LESLIE A. NANGLE, TAMARA L. HENDRICKSON, VALÉRIE DE CRÉCY-LAGARD, PAUL SCHIMMEL, AND PHILIPPE MARLIÈRE

, SCIENCE 20 Apr 2001 Vol 292, Issue 5516 pp. 501-504

More than 20% of the valine in cellular proteins from such an editing mutant organism could be replaced with the noncanonical aminobutyrate, sterically similar to cysteine. Thus, the editing function may have played a central role in restricting the genetic code to 20 amino acids.

Structures and antitumor activities of ten new and twenty known surfactins from the deep-sea bacterium Limimaricola sp. SCSIO 53532

Chen, Min,Chen, Rouwen,Ding, Wenping,Li, Yanqun,Tian, Xinpeng,Yin, Hao,Zhang, Si

, (2022/01/11)

Surfactins are natural biosurfactants wi...

7004-03-7 Process route

C<sub>28</sub>H<sub>41</sub>N<sub>5</sub>O<sub>10</sub>

C28H41N5O10

L-alanin
56-41-7,25191-17-7,18875-37-1

L-alanin

L-valine
72-18-4,25609-85-2,7004-03-7,921-10-8

L-valine

(2R)-aspartic acid
1783-96-6,25608-40-6,27881-03-4,32505-46-7,52526-39-3

(2R)-aspartic acid

Conditions
Conditions Yield
With hydrogenchloride; water; at 120 ℃; for 14h;
 
amantamide

amantamide

L-valine
72-18-4,25609-85-2,7004-03-7,921-10-8

L-valine

L-leucine
61-90-5,21675-61-6,25248-98-0,70-45-1

L-leucine

L-isoleucine
73-32-5,959215-79-3,18875-42-8

L-isoleucine

N-methyl-L-leucine
3060-46-6

N-methyl-L-leucine

N-methyl-D-phenylalanine
56564-52-4

N-methyl-D-phenylalanine

glycine
56-40-6,18875-39-3,25718-94-9

glycine

(-)-α-methylamino-β-methylbutyric acid
88930-14-7

(-)-α-methylamino-β-methylbutyric acid

<i>L</i>-proline
147-85-3,25191-13-3,37159-97-0,4305-67-3,4607-28-7

L-proline

Conditions
Conditions Yield
With hydrogenchloride; In water; at 110 ℃; for 24h;
 

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