Linked Life Data

1021913

Source:http://linkedlifedata.com/resource/pubmed/id/1021913

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1977-5-12
pubmed:abstractText
The activity and stability of some enzymes of Asp. awamori cellulolytic complex were studied as affected by chemical modification of carboxylic groups with N,N'-dicyclohexyl carbodiimide (DCCD) and amine groups with glutaric aldehyde. The carboxylic groups are established to be necessary for manifestation of the activities of C1- and C2-cellulases, Cx-exo- and Cx-endoglucanases. Their role is negligible in the action of beta-glucosidase. The activity of individual cellulases was studied as affected by nucleophilic substitution of DCCD-activated COOH-groups by various reagents (glycine amide, leucine amide, tyrosine amide and N-benzoyl-l-arginine-methyl ether-hydrochloride). Tyrosine amide is the least inacting reagent for all the enzymes, glycine amide is somewhat more activating. Essential differences are shown in the chemical and catalytic properties of Cx-exoglucanase and beta-glucosidase. It is found (under the effect of glutaric aldehyde) that amino groups are significant for manifestation of the activities of C1- and C2-cellulases and Cx-endoglucanase and to a less extent for that of Cs-exoglucanase and beta-glucosidase. It is supposed that electrostatic interactions of the carbolytic and amine groups might be an essential factor for stability of C1- and C2-cellulases and Cx-endoglucanase.
pubmed:language
ukr
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0041-610X
pubmed:author
pubmed:issnType
Print
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
587-91
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
[Modification of the carboxyl and amine groups of the cellulolytic enzymes of Aspergillus awamori].
pubmed:publicationType
Journal Article, English Abstract