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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)

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25 UNITS
$577.00

$577.00

Available to ship onApril 14, 2025Details

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25 UNITS
$577.00

About This Item

CAS Number:
70132-14-8
Enzyme Commission number:
1.4.3.14 (BRENDA, IUBMB)
MDL number:
MFCD00131554
UNSPSC Code:
12352204
NACRES:
NA.54

$577.00

Available to ship onApril 14, 2025Details

biological source

fungus (Trichoderma viride)

Quality Level

200

form

lyophilized powder

specific activity

≥20 units/mg protein

mol wt

112 kDa

composition

Protein, 5-20%

storage temp.

2-8°C

General description

Lysine Oxidase from Trichoderma viride is a homodimeric flavoenzyme corresponding to molecular mass of 112 kDa.[1] It is stable at 65°C and is highly specific for L-lysine substrate.[1] It comprises FAD-binding, substrate binding and a helical domain with distinct active site funnel.[1]

Application

Lysine Oxidase from Trichoderma viride has been used in the preparation of luminescent biochip preparation.[2]

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.[1] It is a tumor suppressor for squamous cell, fibroblast, ovarian and gastric tumors.[3] Lysine oxidase also plays key role in connective tissue structural integrity and embryo development.[3]

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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
0000388257
0000343698
0000336859
0000145471
0000173612

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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.
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
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
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
E V Lukasheva et al.
Voprosy meditsinskoi khimii, 43(6), 566-575 (1998-03-21)
The goal of the present study was the development of the optimal method of co-immobilization of two enzymes: L-lysine alpha-oxidase from Trichoderma sp. and horseradish peroxidase. Commercial nitrocellulose, nylon and N+ nylon membranes were used as carriers. The immobilization was
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