High impact information on Cellvibrio

• The three-dimensional crystal structure of the catalytic module of a "family PL-10" polysaccharide lyase, Pel10Acm from Cellvibrio japonicus, solved at a resolution of 1.3 A, reveals a new polysaccharide lyase fold and is the first example of a polygalacturonic acid lyase that does not exhibit the "parallel beta-helix" topology [1].
• Here we show that the X4 modules from a Cellvibrio japonicus mannanase (Man5C) and arabinofuranosidase (Abf62A) bind to polysaccharides, and thus these proteins comprise a new family of carbohydrate-binding modules (CBMs), designated CBM35 [2].
• Structural and biochemical analysis of Cellvibrio japonicus xylanase 10C: how variation in substrate-binding cleft influences the catalytic profile of family GH-10 xylanases [3].
• The alpha-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants [4].
• Purification and properties of Cellvibrio gilvus cellobiose phosphorylase [5].

Chemical compound and disease context of Cellvibrio

• Instead, it displays a predominantly alpha-helical structure with irregular coils and short beta-strands, similar to the recently reported structure of the catalytic module of the Cellvibrio japonicus pectate lyase Pel10Acm [6].
• Cellvibrio gilvus produced cellulase when grown in the presence of cellulose or carboxymethyl cellulose (CMC) but not when grown in the presence of glucose or cellobiose [7].
• Optimum culture conditions for the epoxidation of cis-propenylphosphonate to fosfomycin by Cellvibrio gilvus [8].
• A cellobiose phosphorylase from Cellvibrio gilvus recognizes only the beta-D-form of 5a-carba-glucopyranose [9].
• Cellobiose phosphorylase from Cellvibrio gilvus was examined for its acceptor specificity in the synthetic reaction with glucose-1-phosphate, using substrates in which the C-6 substituent of D-Glc had been altered [10].

Gene context of Cellvibrio

• In contrast, the beta-glucosidase from Cellvibrio gilvus is mesophilic (35 degrees C) and displays no such transglycosylation activity [11].
• A gene encoding an exo-beta-glucosidase from Cellvibrio mixtus [12].
• Possible roles for a non-modular, thermostable and proteinase-resistant cellulase from the mesophilic aerobic soil bacterium Cellvibrio mixtus [13].

References