Alpha-galactosidase of the marine bacterium Pseudoalteromonas sp. KMM 701.
An alpha-galactosidase that inactivates the group specificity of B erythrocytes (group III) of human blood and does not affect A erythrocytes (group II) was isolated from the marine bacterium Pseudoalteromonas sp. KMM 701. The enzyme preparation did not contain lectin, hemolytic, sialidase, endoglycanase, or glycosidase activities. The enzyme is stable at 20 degreesC for 24 h, has pH optimum for catalysis within the range of 6.7-7.7, and is stable to high concentrations of NaCl. It is 4-fold more efficient than the alpha-galactosidase from green coffee beans. At pH 7.0 the Km for p-nitrophenyl-alpha-D-galactopyranoside is 0.29 mM. The molecular weight of the enzyme determined by gel-filtration is 195 +/- 5 kD. The alpha-galactosidase is denatured by urea and guanidine hydrochloride. Its activity does not depend on the presence of metal ions. It contains a sulfhydryl group essential for its catalytic activity.
Bakunina
I Y
IY
Pacific Institute of Bioorganic Chemistry, Far Eastern Division of the Russian Academy of Sciences, Vladivostok, 690022, Russia. bakun@piboc.marine.su
Sova
V V
VV
Nedashkovskaya
O I
OI
Kuhlmann
R A
RA
Likhosherstov
L M
LM
Martynova
M D
MD
Mihailov
V V
VV
Elyakova
L A
LA
D000017:ABO Blood-Group System / Q000737:chemistry; D002240:Carbohydrate Sequence; D004795:Enzyme Stability; D004912:Erythrocytes / Q000737:chemistry; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012623:Seawater / Q000382:microbiology; D013379:Substrate Specificity; D000519:alpha-Galactosidase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
D000017:ABO Blood-Group System; D000519:alpha-Galactosidase