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A5147

Sigma-Aldrich

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

Type VI, dried venom

Sinónimos:

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

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About This Item

Número de CAS:
9000-89-9
Comisión internacional de enzimas:
1.4.3.2 (BRENDA, IUBMB)
EC Number:
232-564-0
MDL number:
MFCD00131454
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type VI

Quality Level

200

form

dried venom

storage temp.

−20°C

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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
GHS06

signalword

Danger

Hazard Classifications

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

Storage Class

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

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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
Joseph M Boggs et al.
Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases, 12(5), 1005-1009 (2012-03-15)
Phylogenetic analysis of 10 amino acid sequences from 19 Streptococcus species showed that S. oligofermentans clustered within the mitis group. However, the l-amino acid oxidase (LAAO) of S. oligofermentans showed a different clustering pattern from the other proteins analyzed implicating
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
Anwar Ullah et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 68(Pt 2), 211-213 (2012-02-03)
Snake-venom L-amino-acid oxidases (SV-LAAOs) trigger a wide range of local and systematic effects, including inhibition of platelet aggregation, cytotoxicity, haemolysis, apoptosis and haemorrhage. These effects mainly arise from the uncontrolled release of the hydrogen peroxide that is produced by the
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