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A9378

Sigma-Aldrich

L-Amino Acid Oxidase from Crotalus adamanteus

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

Synonym(s):

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

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type IV

Quality Level

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

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.

Packaging

Package size based on protein content

Unit Definition

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

Preparation Note

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

Pictograms

Skull and crossbones

Signal Word

Danger

Hazard Statements

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

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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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
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
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
Chi-Hua Cheng et al.
Analytical biochemistry, 420(1), 93-95 (2011-09-29)
As opposed to single-cell yeast and mammalian cell lines, apoptosis has not been greatly investigated in filamentous fungi because antibodies to the relevant fungal apoptosis-related proteins are not available commercially and because multicellular organisms cannot be studied using flow cytometry.

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