[Isolation, various physico-chemical and catalytic properties of L-methionine-gamma-lyase from Pseudomonas taetrolens].
Homogeneous preparation of L-methionine gamma-lyase was isolated from Ps. taetrolens. As shown by gel filtration and gradient polyacrylamide gel electrophoresis molecular mass of the native L-methionine gamma-lyase was 130-135 kDa. Polyacrylamide gel electrophoresis in presence of 0.1% SDS showed that L-methionine gamma-lyase proved to be a tetramer, which consisted of identical subunits with a molecular mass of 34 kDa. Pyridoxal-5'-phosphate was bound to the enzyme in the ratio of four moles of the cofactor per a mole of protein. The absorption spectrum of the enzyme exhibited maximal values at 420 nm, which is specific for a number of pyridoxal phosphate-containing enzymes. L-methionine gamma-lyase from Ps. taetrolens was found to be dissimilar in its physicochemical and catalytic properties to the same enzymes from other sources.
Zanin
V A
VA
Lukina
V I
VI
Berezov
T T
TT
D013437:Carbon-Sulfur Lyases / Q000302:isolation & purification* / Q000378:metabolism; D002384:Catalysis; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D008190:Lyases / Q000302:isolation & purification*; D011549:Pseudomonas / Q000201:enzymology*; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature
D008190:Lyases; D013437:Carbon-Sulfur Lyases; C021558:L-methionine gamma-lyase
Vydelenie, nekotorye fiziko-khimicheskie i kataliticheskie svoĭstva L-metionin-gamma-liazy iz Pseudomonas taetrolens.