Mechanism: Inverting e: 3D Structure Status ( α / α ) 6 barrel Catalytic Nucleophile/Base: Glu: Catalytic Proton Donor: Glu: External resources: CAZypedia; : Commercial Enzyme Provider(s)

GH78 enzymes hydrolyze glycosidic bonds through an inverting mechanism as elucidated by proton NMR [3, 4]. Typical GH78 α-L-rhamnosidases have molecular masses in the range 80-120 kDa, and are most active at pH 4.0 to 8 and temperature of 50°C against p -nitrophenyl-α-L-rhamnopyranoside [1, 5, 6, 7, 8].

In molecular biology, glycoside hydrolase family 78 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety.

2007年11月23日 · alpha-L-Rhamnosidase (EC 3.2.1.40) catalyzes the hydrolytic release of rhamnose from polysaccharides and glycosides. Bacillus sp. GL1 alpha-L-rhamnosidase (RhaB), a member of glycoside hydrolase (GH) family 78, is responsible for degrading the bacterial biofilm gellan, and also functions as a debitt …

2007年11月23日 · Bacillus sp. GL1 α-L-rhamnosidase (RhaB), a member of glycoside hydrolase (GH) family 78, is responsible for degrading the bacterial biofilm gellan, and also functions as a debittering agent for citrus fruit in the food and beverage industries through the release of rhamnose from plant glycoside, naringin.

Bacillus sp. GL1 alpha-L-rhamnosidase (RhaB), a member of glycoside hydrolase (GH) family 78, is responsible for degrading the bacterial biofilm gellan, and also functions as a debittering agent for citrus fruit in the food and beverage industries through the release of rhamnose from plant glycoside, naringin.

Generally, GH 78 rhamnosidases catalyze the hydrolysis of the glycosidic bond by the inverting mechanism [2,3], in which the aglycone is replaced by a water molecule in a single displacement...

Although both enzymes are members of the same glycosyl hydrolase family (GH 78), our results clearly suggest the distinct functionalities of Ram and Ram2, probably representing two subclasses within GH 78: Ram could efficiently hydrolyze only the synthetic substrate p-nitrophenyl-α-L-rhamnopyranoside (V(max) = 243 U mg(-1)).

We have many unassigned GH, PL, CE, AA, GT, and CBM pages in need of Authors and Responsible Curators. Scientists at all career stages, including students, are welcome to contribute to CAZypedia. Read more here, and in the 10th anniversary article in Glycobiology. New to the CAZy classification? Read this first. *

Enzymes active on complex carbohydrates & glycoconjugates. Purchase CAZy family GH78 …