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Merck

A5147

L-Amino Acid Oxidase from Crotalus atrox (Western Diamondback Rattlesnake)

Type VI, dried venom

Synonyme(s) :

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

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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-564-0
MDL number:
Numéro CE :
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type

Type VI

Quality Level

form

dried venom

storage temp.

−20°C

Application

L-amino acid oxidase is used to convert L-amino acids to their corresponding α-keto acids. Product A5147 is from Crotalus atrox. L-amino acid oxidase, from Sigma, has been used in leucine aminopeptidase (LAP) activity assays .

Biochem/physiol Actions

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 .


pictograms

Skull and crossbones

signalword

Danger

Hazard Classifications

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

Classe de stockage

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

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable



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Contenu apparenté


Saad Alrashdi et al.
Molecules (Basel, Switzerland), 28(1) (2023-01-09)
Indole-containing acyloins are either key intermediates of many antimicrobial/antiviral natural products or building blocks in the synthesis of biologically active molecules. As such, access to structurally diverse indole-containing acyloins has attracted considerable attention. In this report, we present a pilot
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
Hong-Sen Chen et al.
Biochimie, 94(2), 335-344 (2011-08-02)
To investigate the structure-function relationships and geographic variations of L-amino acid oxidase (LAAO) from Daboia venoms, a single LAAO (designated as DrLAO) was purified from eastern Indian Daboia russelii venom and characterized. The purified DrLAO showed subunit molecular mass of



Numéro d'article de commerce international

RéférenceGTIN
A5147-1G04061826297926
A5147-250MG04061833375471
A5147-500MG04061833375488
A5147-100MG04061832727806