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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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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
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
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
Brunna M Okubo et al.
PloS one, 7(3), e33639-e33639 (2012-03-23)
Healthcare-associated infections (HAIs) are causes of mortality and morbidity worldwide. The prevalence of bacterial resistance to common antibiotics has increased in recent years, highlighting the need to develop novel alternatives for controlling these pathogens. Pitviper venoms are composed of a
A Ullah et al.
Biochemical and biophysical research communications, 421(1), 124-128 (2012-04-12)
L-Amino acid oxidases (LAAOs) are flavoenzymes that catalytically deaminate L-amino acids to corresponding α-keto acids with the concomitant production of ammonia (NH(3)) and hydrogen peroxide (H(2)O(2)). Particularly, snake venom LAAOs have been attracted much attention due to their diverse clinical
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