Mutation of a pH-modulating residue in a GH51 α-l-arabinofuranosidase leads to a severe reduction of the secondary hydrolysis of transfuranosylation products.
Biochim Biophys Acta
; 1840(1): 626-36, 2014 Jan.
Article
in En
| MEDLINE
| ID: mdl-24140392
Key words
4-nitrochatecol α-l-arabinofuranoside; 4NTC-α-l-Araf; AXOS; Abfs; FH; GH; KIE; Pentoses/furanoses; R(T); STD NMR; Saturation Transfer Difference Nuclear Magnetic Resonance; T/H ratio; Transglycosylation; TxAbf; TxAbf(Ç); X; Y; arabinoxylo-oligosaccharides; d-Xylp; d-xylopyranosyl; donor conversion rate; furanoside hydrolase; glycoside hydrolase; inactivated form (E176A) of TxAbf; kinetic isotope effects; l-Araf; l-arabinofuranosyl; mNP; meta-nitrophenol; oNP; ortho-nitrophenol; pH-dependent inhibition; pK(a) modulation; pNP; pNP-α-l-Araf; para-nitrophenol; para-nitrophenyl α-l-arabinofuranoside; transfer rate; transglycosylation/hydrolysis ratio; yield; α-l-arabinofuranosidase from Thermobacillus xylanilyticus; α-l-arabinofuranosidases
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Arabinose
/
Bacillaceae
/
Glycoside Hydrolases
/
Mutation
Language:
En
Journal:
Biochim Biophys Acta
Year:
2014
Document type:
Article
Affiliation country:
Francia
Country of publication:
Países Bajos