Beta-galactosidase from psychrotrophic microorganism (strain Arthrobacter)

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F04%3A00012746" target="_blank" >RIV/60461373:22330/04:00012746 - isvavai.cz</a>

Alternative codes found

RIV/61389013:_____/04:00101440

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Beta-galactosidase from psychrotrophic microorganism (strain Arthrobacter)

Original language description

The ß-galactosidase from Arthrobacter sp. C2-2, main subject of this study, was derived from bacteria living in Antarctica under low temperatures (permanently below 5 C). Its low temperature activity deserves special attention because of many practical and theoretical impacts of enzymatic processes under ambient temperatures [1,2]. The elucidation of low temperature adaptation of enzymes requires knowledge of detailed molecular geometry and an analysis of conformational changes in the active site. The only known method being able to give complete determination of structure of large proteins is the X-ray crystallography. Therefore, the first part of our project is to determine the structure the above mentioned cold-active enzyme using X-ray diffraction.Cold active ß-galactosidase from Arthrobacter sp. C2-2 is a large protein - homotetramer with molecular weight 500 kDa, having 4092 residues. It is homological to the ß-galactosidase from Escherichia coli (sequence identity 32%). Expressi

Czech name

Beta-galaktosidasa z psychrofilního mikroorganismu (kmene Arthrobacter)

Czech description

Beta-galaktosidasa z psychrofilního mikroorganismu (kmene Arthrobacter)

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

<a href="/en/project/GA204%2F02%2F0843" target="_blank" >GA204/02/0843: Complex cold adaptation study of enzymes on molecular level and their application in biotechnology</a><br>

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2004

Confidentiality

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

Name of the periodical

Mater. Struct.

ISSN

1211-5894

e-ISSN

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Volume of the periodical

11

Issue of the periodical within the volume

1

Country of publishing house

CZ - CZECH REPUBLIC

Number of pages

2

Pages from-to

18-19

UT code for WoS article

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EID of the result in the Scopus database

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