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L6150

Sigma-Aldrich

Lysine Oxidase from Trichoderma viride

lyophilized powder, ≥20 units/mg protein

Synonym(s):
L-Lysine:oxygen oxidoreductase (deaminating)
CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.54

biological source

fungus (Trichoderma viride)

Quality Level

form

lyophilized powder

specific activity

≥20 units/mg protein

mol wt

112 kDa

composition

Protein, 5-20%

storage temp.

2-8°C

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This Item
L5135X3876A9378
form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

aqueous suspension

specific activity

≥20 units/mg protein

specific activity

≥60 units/mg protein

specific activity

100-300 units/mg protein

specific activity

≥4.0 units/mg protein

mol wt

112 kDa

mol wt

245 kDa

mol wt

22 kDa

mol wt

~130 kDa

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

-

General description

Lysine Oxidase from Trichoderma viride is a homodimeric flavoenzyme corresponding to molecular mass of 112 kDa. It is stable at 65°C and is highly specific for L-lysine substrate. It comprises FAD-binding, substrate binding and a helical domain with distinct active site funnel.

Application

Lysine Oxidase from Trichoderma viride has been used in the preparation of luminescent biochip preparation.

Biochem/physiol Actions

Lysine Oxidase from Trichoderma viride catalyzes the formation of α-keto- ε-aminocaproate by the oxidative deamination of L-lysine. It displays anti-tumor functionality in cancer leukaemic cells. It is a tumor suppressor for squamous cell, fibroblast, ovarian and gastric tumors. Lysine oxidase also plays key role in connective tissue structural integrity and embryo development.

Unit Definition

One unit will catalyze the formation of 1 μmole of 6-amino-2-oxohexanoic acid from L-lysine per min at 37°C at pH 8.0.

Physical form

Contains phosphate buffer salts and stabilizer

Storage Class Code

11 - Combustible Solids

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)

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25G
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I P Smirnova et al.
Voprosy meditsinskoi khimii, 46(4), 384-387 (2000-11-15)
The ability of protein isolated from (Trichoderma Rifai) and azydothymidine to inhibit the reproduction of HIV-virus was compared. The obtained experimental data have verified that Trichoderma Rifai protein is a promising human immunodeficiency virus (HIV) inhibitor.
O S Zhukova et al.
Voprosy meditsinskoi khimii, 47(6), 588-592 (2002-04-03)
The conjugates of L-lysine alpha-oxidase and monoclonal antibodies ICO-80 towards CD-5 receptor were produced using glutaraldehyde. The cytotoxic effect of conjugates on Yurkat cells line appeared to be lower in comparison with the native enzyme. Negligible decrease of conjugate biological
Recombinant expression, molecular characterization and crystal structure of antitumor enzyme, l-lysine alpha-oxidase from Trichoderma viride
Amano M, et al.
The Journal of Biological Chemistry, 157(6), 549-559 (2015)
Seiji Okazaki et al.
Journal of biochemistry, 154(3), 233-236 (2013-08-03)
We have determined the x-ray crystal structure of L-lysine ε-oxidase from Marinomonas mediterranea in its native and L-lysine-complex forms at 1.94- and 1.99-Å resolution, respectively. In the native enzyme, electron densities clearly indicate the presence of cysteine tryptophylquinone (CTQ) previously
E V Lukasheva et al.
Biochemistry. Biokhimiia, 67(10), 1152-1158 (2002-12-04)
This review summarizes data on the properties of L-lysine alpha-oxidase, an enzyme that belongs to the group of oxidases of L-amino acids. This enzyme acts virtually only on L-lysine with a rather low Km yielding alpha-keto-epsilon-aminocaproic acid. The decrease in

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