A5147
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:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-564-0
MDL number:
Product Name
L-Amino Acid Oxidase from Crotalus atrox (Western Diamondback Rattlesnake), Type VI, dried venom
type
Type VI
form
dried venom
storage temp.
−20°C
Quality Level
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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 .
signalword
Danger
hcodes
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
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
低风险生物材料
动植物源性产品
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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
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
Chi-Hua Cheng et al.
Journal of agricultural and food chemistry, 59(17), 9142-9149 (2011-07-30)
L-amino acid oxidases (L-AAOs) have been isolated from many organisms, such as snake, and are known to have antibacterial activity. To the best of the authors' knowledge, this is the first report of the cloning of cDNA encoding a novel
Ko-Chun Ko et al.
Antimicrobial agents and chemotherapy, 56(4), 1725-1734 (2012-01-11)
The marine snail Aplysia californica produces escapin, an L-amino acid oxidase, in its defensive ink. Escapin uses L-lysine to produce diverse products called escapin intermediate products of L-lysine (EIP-K), including α-amino-ε-caproic acid, Δ¹-piperidine-2-carboxylic acid, and Δ²-piperidine-2-carboxylic acid. EIP-K and H₂O₂
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