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Key Documents

A9378

Sigma-Aldrich

L-Amino Acid Oxidase from Crotalus adamanteus

Type IV, ≥4.0 units/mg protein, aqueous suspension

Synonyme(s) :

L-AAO, L-Amino acid:oxygen oxidoreductase (deaminating)

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Type

Type IV

Forme

aqueous suspension

Activité spécifique

≥4.0 units/mg protein

Poids mol.

~130 kDa

Contient

toluene as preservative

Concentration

≥5.0 mg/mL

Solubilité

H2O: soluble 1.0 mg/mL, clear

Température de stockage

2-8°C

Application

L-amino acid oxidase (LAAO) is used to convert L-amino acids to their corresponding α-keto acids. L-amino acid oxidase, from Sigma, has been used in leucine aminopeptidase (LAP) activity assays. 35S dimethylsulfoniopropionate (DMSP) has been synthesized chemically from 35S L-methionine using LAAO from Sigma to form 35S 3-methiolpropionate.

Actions biochimiques/physiologiques

L-Amino acid oxidase is a flavoprotein with a molecular weight of 130 kDa. It consists of two different subunits of approximately 70,000 Da. Each molecule of holoenzyme has two FAD molecules. It is a glycoprotein containing about 2-5% carbohydrate, including sialic acid. Optimum pH is approximately 7.5.The enzyme may be reversibly inactivated by incubation in phosphate buffer, pH 7.5 at 38 °C. L-amino acid oxidase is involved in various metabolic pathways such as alanine and aspartate metabolism, methionine metabolism, valine, leucine and isoleucine degradation, tyrosine metabolism, phenylalanine metabolism, tryptophan metabolism, phenylalanine, tyrosine and tryptophan biosynthesis, and alkaloid biosynthesis. It occurs in many snake venoms apart from microorganisms and animal tissue, especially in kidney and liver.

Conditionnement

Package size based on protein content

Définition de l'unité

One Unit oxidizes one micromole of L-leucine per minute at 25 °C, pH 7.6

Notes préparatoires

Dissolves in water at 1 mg/mL concentration to form a clear solution.

Pictogrammes

Skull and crossbones

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

Acute Tox. 1 Inhalation - Acute Tox. 2 Dermal - Acute Tox. 2 Oral

Code de la classe de stockage

6.1A - Combustible acute toxic Cat. 1 and 2 / very toxic hazardous materials

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Identification and enumeration of bacteria assimilating dimethylsulfoniopropionate (DMSP) in the North Atlantic and Gulf of Mexico
Malmstrom RR, et al.
Limnology and Oceanography, 49(2), 597-606 (2004)
Stefania Digiovanni et al.
Scientific reports, 10(1), 10135-10135 (2020-06-25)
Reactive Intermediate Deaminase (Rid) protein superfamily includes eight families among which the RidA is conserved in all domains of life. RidA proteins accelerate the deamination of the reactive 2-aminoacrylate (2AA), an enamine produced by some pyridoxal phosphate (PLP)-dependent enzymes. 2AA
Jiro Arima et al.
The Journal of biological chemistry, 281(9), 5885-5894 (2006-01-13)
Streptomyces griseus leucine aminopeptidase (SGAP), which has two zinc atoms in its active site, is clinically important as a model for understanding the structure and mechanism of action of other metallopeptidases. SGAP is a calcium-activated and calcium-stabilized enzyme, and its
Paola Rey-Suárez et al.
Journal of proteomics, 75(2), 655-667 (2011-10-04)
Venoms of the redtail coral snake Micrurus mipartitus from Colombia and Costa Rica were analyzed by "venomics", a proteomic strategy to determine their composition. Proteins were separated by RP-HPLC, followed by SDS-PAGE, in-gel tryptic digestion, identification by MALDI or ESI
R L Hanson et al.
Enzyme and microbial technology, 48(6-7), 445-453 (2011-11-25)
N-Cbz-4,5-dehydro-L-prolineamide or N-Boc-4,5-dehydro-L-prolineamide are alternative key intermediates for the synthesis of saxagliptin, a dipeptidyl peptidase IV (DPP4) inhibitor recently approved for treatment of type 2 diabetes mellitus. An efficient biocatalytic method was developed for conversion of L-ornithine, N-α-benzyloxycarbonyl (Cbz)-L-ornthine, and

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