The alpha-galactosidase type A gene aglA from Aspergillus niger encodes a fully functional alpha-N-acetylgalactosaminidase

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F10%3A00355844" target="_blank" >RIV/61388971:_____/10:00355844 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67179843:_____/10:00355844 RIV/67985556:_____/10:00355844 RIV/60076658:12640/10:00012176

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

The alpha-galactosidase type A gene aglA from Aspergillus niger encodes a fully functional alpha-N-acetylgalactosaminidase

Popis výsledku v původním jazyce

Two genes in the genome of Aspergillus niger, aglA and aglB, have been assigned to encode for ?-d-galactosidases variant A and B. However, analyses of primary and 3D structures based on structural models of these two enzymes revealed significant differences in their active centers suggesting important differences in their specificity for the hydrolyzed carbohydrates. To test this unexpected finding, a large screening of libraries from 42 strains of filamentous fungi succeeded in identifying an enzyme from A. niger CCIM K2 that exhibited both ?-galactosidase and?-N-acetylgalactosaminidase activities, with the latter activity predominating. The enzyme protein was sequenced, and its amino acid sequence could be unequivocally assigned to the enzyme encodedthe aglA gene. Enzyme activity measurements and substrate docking clearly demonstrated the preference of the identified enzyme for ?-N-acetyl-d-galactosaminide over ?-d-galactoside.

Název v anglickém jazyce

The alpha-galactosidase type A gene aglA from Aspergillus niger encodes a fully functional alpha-N-acetylgalactosaminidase

Popis výsledku anglicky

Two genes in the genome of Aspergillus niger, aglA and aglB, have been assigned to encode for ?-d-galactosidases variant A and B. However, analyses of primary and 3D structures based on structural models of these two enzymes revealed significant differences in their active centers suggesting important differences in their specificity for the hydrolyzed carbohydrates. To test this unexpected finding, a large screening of libraries from 42 strains of filamentous fungi succeeded in identifying an enzyme from A. niger CCIM K2 that exhibited both ?-galactosidase and?-N-acetylgalactosaminidase activities, with the latter activity predominating. The enzyme protein was sequenced, and its amino acid sequence could be unequivocally assigned to the enzyme encodedthe aglA gene. Enzyme activity measurements and substrate docking clearly demonstrated the preference of the identified enzyme for ?-N-acetyl-d-galactosaminide over ?-d-galactoside.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2010

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Glycobiology

ISSN

0959-6658

e-ISSN

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Svazek periodika

20

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

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Kód UT WoS článku

000282750300009

EID výsledku v databázi Scopus

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