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A5147

Sigma-Aldrich

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

Type VI, dried venom

Synonym(s):

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

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About This Item

CAS Number:
9000-89-9
Enzyme Commission number:
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

Signal Word

Danger

Hazard Statements

H300 + H310 + H330

Hazard Classifications

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

Storage Class Code

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘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
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
Zhiliang Yu et al.
Applied biochemistry and biotechnology, 167(1), 1-13 (2012-03-01)
L-amino acid oxidase is widely found in diverse organisms and has different properties. It is thought to contribute to antimicrobial activity, amino acid catabolism, and so forth. The purpose of this communication is to summarize the advances in non-snake venom
Chia-Ann Yang et al.
Journal of agricultural and food chemistry, 60(10), 2464-2471 (2012-02-23)
The monomeric L-amino acid oxidase (mTh-LAAO) of Trichoderma harzianum ETS 323 has been suggested to antagonize Rhizoctonia solani by an unknown mechanism. Here, the mTh-LAAO-treated R. solani exhibited hyphal lysis and apoptotic characteristics such as DNA fragmentation, reactive oxygen species
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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