Literature summary for 3.2.1.40 extracted from

ONeill, E.C.; Stevenson, C.E.; Paterson, M.J.; Rejzek, M.; Chauvin, A.L.; Lawson, D.M.; Field, R.A.
Crystal structure of a novel two domain GH78 family alpha-rhamnosidase from Klebsiella oxytoca with rhamnose bound (2015), Proteins, 83, 1742-1749 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method, crystal structure is determined at 2.7 A resolution with rhamnose bound in the active site of the catalytic domain. The homodimeric structure is significantly smaller than those of the other previously determined GH78 structures. Nevertheless, the enzyme displays alpha-rhamnosidase activity when assayed in vitro, suggesting that the additional structural domains found in the related enzymes are dispensible for function	Klebsiella oxytoca

Crystallization (Comment)

Organism

hanging drop vapor diffusion method, crystal structure is determined at 2.7 A resolution with rhamnose bound in the active site of the catalytic domain. The homodimeric structure is significantly smaller than those of the other previously determined GH78 structures. Nevertheless, the enzyme displays alpha-rhamnosidase activity when assayed in vitro, suggesting that the additional structural domains found in the related enzymes are dispensible for function

Klebsiella oxytoca

Organism

Organism	UniProt	Comment	Textmining
Klebsiella oxytoca	A0A0J9X262	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Klebsiella oxytoca

Synonyms

Synonyms	Comment	Organism
KoRha	-	Klebsiella oxytoca

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Release 2023.1 (January 2023)