A5147

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

Name: <SC>L</SC>-Amino Acid Oxidase from <I>Crotalus atrox</I> (Western Diamondback Rattlesnake)
Brand: SIGMA
Price: 113 USD

Type VI, dried venom

Synonym(s):

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

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100 MG

$113.00

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$189.00

500 MG

$331.00

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$591.00

$113.00

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About This Item

CAS Number:

9000-89-9

UNSPSC Code:

12352204

NACRES:

NA.54

EC Number:

232-564-0

MDL number:

MFCD00131454

EC Number:

1.4.3.2 (BRENDA, IUBMB)

Key Documents

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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

200

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Show Differences

1 of 4

This Item	P4506	A9253	A9378
Sigma-Aldrich A5147 L-Amino Acid Oxidase from Crotalus atrox (Western Diamondback Rattlesnake)	Sigma-Aldrich P4506 Phosphodiesterase I from Crotalus atrox (Western Diamondback Rattlesnake)	Sigma-Aldrich A9253 L-Amino Acid Oxidase from Crotalus adamanteus	Sigma-Aldrich A9378 L-Amino Acid Oxidase from Crotalus adamanteus
form dried venom	form crude dried venom	form powder	form aqueous suspension
storage temp. −20°C	storage temp. −20°C	storage temp. −20°C	storage temp. 2-8°C
Quality Level 200	Quality Level 200	Quality Level 200	Quality Level 200
type Type VI	type Type IV	type Type I (dried venom)	type Type IV

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 [1].

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 [2].

pictograms

GHS06

signalword

Danger

hcodes

H300 + H310 + H330

pcodes

P260 - P262 - P264 - P280 - P302 + P352 + P310 - P304 + P340 + P310

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

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Chemoenzymatic Synthesis of Indole-Containing Acyloin Derivatives.

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

Modulation of Streptomyces leucine aminopeptidase by calcium: identification and functional analysis of key residues in activation and stabilization by calcium.

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

Cloning, characterization and mutagenesis of Russell's viper venom L-amino acid oxidase: Insights into its catalytic mechanism.

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

Phylogenetic analysis supports horizontal gene transfer of L-amino acid oxidase gene in Streptococcus oligofermentans.

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

Enzymatic preparation of 5-hydroxy-L-proline, N-Cbz-5-hydroxy-L-proline, and N-Boc-5-hydroxy-L-proline from (α-N-protected)-L-ornithine using a transaminase or an amine oxidase.

R L Hanson et al.

Enzyme and microbial technology, 48(6-7), 445-453 (2011-11-25)

N-Cbz-4,5-dehydro-L-prolineamide or N-Boc-4,5-dehydro-L-prolineamide are alternative key intermediates for the synthesis of saxagliptin, a dipeptidyl peptidase IV (DPP4) inhibitor recently approved for treatment of type 2 diabetes mellitus. An efficient biocatalytic method was developed for conversion of L-ornithine, N-α-benzyloxycarbonyl (Cbz)-L-ornthine, and

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