N-Acetyl L-Glutamine Nutrition Supplement Aceglutamide

N-Acetyl L-Glutamine CAS 2490-97-3 Nutrition Supplement Aceglutamide N-Acetyl L-Glutamine Quick Details: CAS No.:56-85-9 Other Names:L-Glutamine MF:C5H10N2O3 EINECS No.:200-292-1 Place of Origin:China (Mainland) Type:Vitamins, Amino...
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Product Details

N-Acetyl L-Glutamine CAS 2490-97-3 Nutrition Supplement Aceglutamide


N-Acetyl L-Glutamine 

Quick Details:

CAS No.:56-85-9

Other Names:L-Glutamine

MF:C5H10N2O3

EINECS No.:200-292-1

Place of Origin:China (Mainland)

Type:Vitamins, Amino Acids and Coenzymes, L-Glutamine

Grade Standard:Cosmetic Grade, Food Grade, Medicine Grade

Brand Name: SENDI

Model Number:USP39

Purity:99.9%min

Product Name:Pharma Grade Glutamine Powder Bulk

Appearance:White crystalline powder

HS Code:29241900

Assay(%):99- 101.5%

Loss on drying(%):0.3 Max

Shelf life:2 Years

Package:20 KG/CTN

Certificate:ISO,HALAL,KOSHER


Product NamePharma Grade Glutamine Powder Bulk


1.Appearance: White crystals or crystalline powder 
2.Package: 25 KG/DRUM ,11Mt/20'FCL
3. CAS No.: 56-85-9
4. Shelf life:24 months

 

Glutamine Powder is the most abundant amino acid found in human muscle and plasma. Over 60% of the free-floating amino acid pool in skeletal muscle cells is made up of L glutamine. It is also a primary nitrogen donor, meaning that it moves the nitrogen around in the body to where it is needed. Maintaining a positive nitrogen balance is absolutely necessary for muscle building.

 

Product Specification Of L-Glutamine 

ItemsStandards
AppearanceWhite crystalline powder
IdenfificationPositive
Specific Rotation(°)+6.3 - +7.3
Assay(%)99.5 - 101.5
Loss on drying(%)0.3 Max
Residue on ignition(%)0.1 Max
Heavy Metals(ppm)10 Max

Packaging: 25 KG/DRUM

Shelf life: 2 YEARS

Storage:Kept in dry, cool, and shaded place with original packaging, avoid moisture, store at room temperature.

 

Product Specification Of L-Glutamine 

ItemsStandards
AppearanceWhite crystalline powder
IdenfificationPositive
Specific Rotation(°)+6.3 - +7.3
Assay(%)99 - 101.5
Loss on drying(%)0.3 Max
Residue on ignition(%)0.3 Max
Heavy Metals(ppm)15 Max
Fe(ppm)30 Max
Cl(%)0.05 Max
SO4(%)0.03 Max
Other amino acid(%)0.50 Max

Conclusion: The Goods Conform to the standards of USP35.

Packaging: 25 KG/DRUM

Shelf life: 2 YEARS

Storage:Kept in dry, cool, and shaded place with original packaging, avoid moisture, store at room temperature.

 

Fuction Of L-Glutamine:

1. L-Glutamine is the most prevalent amino acid in the bloodstream. 
2. L-Glutamine is involved in more metabolic processes than any other amino acid. 
3. L-Glutamine is converted to glucose when more glucose is required by the body as an energy source. 
4. L-Glutamine also plays a part in maintaining proper blood glucose levels and the right pH range. 
5. L-Glutamine serves as a source of fuel for cells lining the intestines. Without it, these cells waste away. 
6. L-Glutamine is also used by white blood cells and is important for immune function.

Biological function

Most prokaryotes (bacteria) and lower eukaryotes (fungi, green algae, plants, etc.) produce NAG through orinithine acetyltransferase (OAT), which is part of a ‘cyclic’ ornithine production pathway. NAGS is therefore used in a supportive role, replenishing NAG reserves as required. In some plants and bacteria, however, NAGS catalyzes the first step in a ‘linear’ arginine production pathway.


The protein sequences of NAGS between prokaryotes, lower eukaryotes and higher eukaryotes have shown a remarkable lack of similarity. Sequence identity between prokaryotic and eukaryotic NAGS is largely <30%,[3] while sequence identity between lower and higher eukaryotes is ~20%.


Enzyme activity of NAGS is modulated by L-arginine, which acts as an inhibitor in plant and bacterial NAGS, but an effector in vertebrates. While the role of arginine as an inhibitor of NAG in ornithine and arginine synthesis is well understood, there is some controversy as to the role of NAG in the urea cycle.[7][8] The currently accepted role of NAG in vertebrates is as an essential allosteric cofactor for CPS1, and therefore it acts as the primary controller of flux through the urea cycle. In this role, feedback regulation from arginine would act to signal NAGS that ammonia is plentiful within the cell, and needs to be removed, accelerating NAGS function. As it stands, the evolutionary journey of NAGS from essential synthetic enzyme to primary urea cycle controller is yet to be fully understood.


Mechanism


A simplified reaction mechanism for N-Acetylglutamate synthase (NAGS)

Two mechanisms for N-acetyltransferase function have been proposed: a two-step, ping-pong mechanism involving transfer of the relevant acetyl group to an activated cysteine residue and a one-step mechanism through direct attack of the amino nitrogen on the carbonyl group. Studies conducted using NAGS derived from Neisseria gonorrhoeae suggest that NAGS proceeds through the previously described one-step mechanism. In this proposal, the carbonyl group of acetyl-CoA is attacked directly by the α-amino nitrogen of glutamate. This mechanism is supported by the activation of the carbonyl through hydrogen bond polarization, as well as the absence of a suitable cysteine within the active site to act as an intermediate acceptor of the acetyl group.


Clinical significance

Inactivity of NAGS results in N-acetylglutamate synthase deficiency, a form of hyperammonemia. In many vertebrates, N-acetylglutamate is an essential allosteric cofactor of CPS1, the enzyme that catalyzes the first step of the urea cycle. Without NAG stimulation, CPS1 cannot convert ammonia to carbamoyl phosphate, resulting in toxic ammonia accumulation. Carbamoyl glutamate has shown promise as a possible treatment for NAGS deficiency. This is suspected to be a result of the structural similarities between NAG and carabamoyl glutamate, which allows carbamoyl glutamate to act as an effective agonist for CPS1.



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