The endo-beta-agarases AgaA and AgaB from the marine bacterium Zobellia galactanivorans: two paralogue enzymes with different molecular organizations and catalytic behaviours.
Jam
Murielle
M
Végétaux Marins et Biomolécules, UMR 7139 (CNRS/UPMC/Goëmar), Station Biologique, Place Georges Teissier, BP 74, 29682 Roscoff Cedex, Bretagne, France.
Flament
Didier
D
Allouch
Julie
J
Potin
Philippe
P
Thion
Laurent
L
Kloareg
Bernard
B
Czjzek
Mirjam
M
Helbert
William
W
Michel
Gurvan
G
Barbeyron
Tristan
T
D000595:Amino Acid Sequence; D001483:Base Sequence; D002384:Catalysis; D020134:Catalytic Domain; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D041965:Flavobacteriaceae / Q000201:enzymology* / Q000235:genetics; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy; D008386:Marine Biology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D044367:Phase Transition; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D012685:Sepharose / Q000737:chemistry / Q000378:metabolism; D021241:Spectrometry, Mass, Electrospray Ionization; D013379:Substrate Specificity
D011994:Recombinant Proteins; D012685:Sepharose; D006026:Glycoside Hydrolases; C019624:agarase