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ChemicalBook--->CAS DataBase List--->9000-89-9

9000-89-9

9000-89-9 Structure

9000-89-9 Structure
IdentificationBack Directory
[Name]

L-Amino Acid Oxidase
[CAS]

9000-89-9
[Synonyms]

L-AAO
TM-LAO
EC 1.4.3.2
IUB: 1.4.3.2
l-aminooxidase
oxidase,l-aminoacid
L-AMINO ACID OXIDASE
AMINO ACID OXIDASE, L-
aromaticl-aminoacidoxidase
L-AMINO ACID OXIDASE TYPE I
L-AMINO ACID OXIDASE TYPE II
L-AMINO ACID OXIDASE TYPE IV
L-AMINO ACID OXIDASE TYPE VI
L-AMino acid oxidase >4 U/Mg
D-AminoAcidOxidaseExPigKidney
oxygen oxidoreductase(deaminating)
L-AMINO ACID:OXYGEN OXIDOREDUCTASE
L-AMINO ACID OXIDASE FROM CROTALUS DURIS
l-aminoacidoxidasefromcrotalusada-manteus
Native Crotalus atrox L-Amino Acid Oxidase
l-amino acid oxidase from bothrops atrox venom
Native Crotalus adamanteus L-Amino Acid Oxidase
L-AMINO ACID: OXYGEN OXIDOREDUCTASE [DEAMINATING]
L-AMINO ACID OXIDASE TYPE II CRUDEDRIED VENOM FROM
L-AMINO ACID OXIDASE TYPE VI CRUDEDRIED VENOM FROM
L-AMINO-ACID OXIDASE TYPE I CRUDE DRIED VENOM FROM
Native Crotalus durissus venom L-Amino Acid Oxidase
L-AMINO ACID OXIDASE TYPE IV:PURIFIED FR OM CROTALU
L-AMINO ACID OXIDASE FROM CROTALUS ATROX , ~0.3 U/MG
L-AMINO ACID OXIDASE, FROM CROTALUS ADAMANTEUS VENOM
L-Amino Acid Oxidase from Crotalus durissus venom
L-AMINO ACID: OXYGEN OXIDOREDUCTASE [DEAMINATING] TYPE II
L-AMINO ACID: OXYGEN OXIDOREDUCTASE [DEAMINATING] TYPE IV
L-AMINO ACID: OXYGEN OXIDOREDUCTASE [DEAMINATING] TYPE VI
L-AMINO ACID OXIDASE FROM CROTALUS ADA-M ANTEUS, ~0.5 U/MG
L-AAO, L-Amino acid: oxygen oxidoreductase (deaminating)
l-amino acid oxidase from crotalus atrox (western diamondback rattlesnake)
[EINECS(EC#)]

232-564-0
[MDL Number]

MFCD00131454
Chemical PropertiesBack Directory
[storage temp. ]

2-8°C
[solubility ]

H2O: soluble1.0mg/mL, clear(lit.)
[form ]

powder
[color ]

yellow
[biological source]

Crotalus adamanteus
[Water Solubility ]

H2O: soluble 1.0mg/mL, clear(lit.)
[Merck ]

13,414
[Specific Activity]

≥4.0units/mg protein
Safety DataBack Directory
[Hazard Codes ]

T+
[Risk Statements ]

26/27/28
[Safety Statements ]

36/37/39-45
[RIDADR ]

UN 3462 6.1/PG 1
[WGK Germany ]

3
[RTECS ]

RQ8300000
[F ]

10-18-21
[HazardClass ]

6.1(b)
[PackingGroup ]

III
Hazard InformationBack Directory
[Uses]

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.
[Uses]

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.
[Uses]

L-Amino Acid Oxidase from Crotalus adamanteus has been used in the quantification of rid protein in imine deaminase activity.
[General Description]

L-Amino acid oxidase (LAAO) is a flavoprotein with a molecular weight of 130 kDa. It consists of two different subunits of approximately 70 kDa. Each molecule of holoenzyme has two flavin adenine dinucleotide (FAD) molecules. LAAO is a glycoprotein containing about 2-5% carbohydrate, including sialic acid. optimum pH is approximately 7.5. It occurs in many snake venoms apart from microorganisms and animal tissue, especially in kidney. In the N-terminal region, it has a βαβ domain with glutamic acid residues. LAAO imparts yellow color to venom.
[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.
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