[A comparative study of the physico-chemical properties of lysine oxidase from Trichoderma sp. and Trichoderma viride Y 244-2].
Some physicochemical properties of L-lysine oxidase from two strains of Trichoderma were studied. Content of metals and cofactors (Se, Zn, Cu, Fe, Co, Mn, Mo), amino acid analysis, secondary structure were estimated. The enzyme molecule from Trichoderma sp was found to contain both FAD and PQQ cofactors.
Khaduev
S Kh
SKh
Lukasheva
E V
EV
Vesa
V S
VS
Oĭkava
T
T
Esaki
N
N
Soda
K
K
Adachi
O
O
Iagi
K
K
Berezov
T T
TT
D000594:Amino Acid Oxidoreductases / Q000737:chemistry*; D000596:Amino Acids / Q000032:analysis; D002850:Chromatography, Gel; D002942:Circular Dichroism; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry; D045542:PQQ Cofactor; D015363:Quinolones / Q000737:chemistry; D013045:Species Specificity; D013050:Spectrometry, Fluorescence; D014242:Trichoderma / Q000201:enzymology*
D000596:Amino Acids; D015363:Quinolones; D005182:Flavin-Adenine Dinucleotide; D045542:PQQ Cofactor; D000594:Amino Acid Oxidoreductases; C041123:L-lysine oxidase
Sravnietl'noe issledovanie fiziko-khimicheskikh svoĭstv lizinoksidazy iz Trichoderma sp. i Trichoderma viride Y 244-2.