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Merck
CN

A9378

L-Amino Acid Oxidase from Crotalus adamanteus

Type IV, ≥4.0 units/mg protein, aqueous suspension

别名:

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

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化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-564-0
MDL number:
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产品名称

L-Amino Acid Oxidase from Crotalus adamanteus, Type IV, ≥4.0 units/mg protein, aqueous suspension

type

Type IV

form

aqueous suspension

specific activity

≥4.0 units/mg protein

mol wt

~130 kDa

contains

toluene as preservative

concentration

≥5.0 mg/mL

solubility

H2O: soluble 1.0 mg/mL, clear

storage temp.

2-8°C

Quality Level

Application

L-amino acid oxidase (LAAO) is used to convert L-amino acids to their corresponding α-keto acids. L-amino acid oxidase, from Sigma, has been used in leucine aminopeptidase (LAP) activity assays. 35S dimethylsulfoniopropionate (DMSP) has been synthesized chemically from 35S L-methionine using LAAO from Sigma to form 35S 3-methiolpropionate.

Biochem/physiol Actions

L-Amino acid oxidase is a flavoprotein with a molecular weight of 130 kDa. It consists of two different subunits of approximately 70,000 Da. Each molecule of holoenzyme has two FAD molecules. It is a glycoprotein containing about 2-5% carbohydrate, including sialic acid. Optimum pH is approximately 7.5.The enzyme may be reversibly inactivated by incubation in phosphate buffer, pH 7.5 at 38 °C. 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. It occurs in many snake venoms apart from microorganisms and animal tissue, especially in kidney and liver.

Other Notes

One Unit oxidizes one micromole of L-leucine per minute at 25 °C, pH 7.6

Packaging

Package size based on protein content

Preparation Note

Dissolves in water at 1 mg/mL concentration to form a clear solution.

pictograms

Skull and crossbones

signalword

Danger

Hazard Classifications

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

存储类别

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

ppe

Eyeshields, Gloves, type N95 (US)

法规信息

动植物源性产品
低风险生物材料
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Identification and enumeration of bacteria assimilating dimethylsulfoniopropionate (DMSP) in the North Atlantic and Gulf of Mexico
Malmstrom RR, et al.
Limnology and Oceanography, 49(2), 597-606 (2004)
Stefania Digiovanni et al.
Scientific reports, 10(1), 10135-10135 (2020-06-25)
Reactive Intermediate Deaminase (Rid) protein superfamily includes eight families among which the RidA is conserved in all domains of life. RidA proteins accelerate the deamination of the reactive 2-aminoacrylate (2AA), an enamine produced by some pyridoxal phosphate (PLP)-dependent enzymes. 2AA
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
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
Koh Ida et al.
Journal of biochemistry, 150(6), 659-669 (2011-08-16)
The mature form of L-Phe oxidase of Pseudomonas sp. P-501 (PAOpt) catalyzes the oxygenative decarboxylation of L-Phe and the oxidative deamination of L-Met, and is highly specific for L-Phe. The crystal structures of PAOpt individually complexed with L-Phe and L-Met

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