Literature summary for 3.2.1.49 extracted from

Meshach Paul, D.; Rajasekaran, R.
Exploration of structural and functional variations owing to point mutations in alpha-NAGA (2018), Interdiscip. Sci., 10, 81-92 .

Search for more literature for 3.2.1.49

Protein Variants

Protein Variants	Comment	Organism
E325K	less favourable binding energy compared to native enzyme. The mutant enzyme possesses reduced volume in the catalytic cleft as compared to native enzyme resulting in the change in substrate pose. Changes in root mean square fluctuation of residues involved in catalytic activity affects the active site in terms of conformational space, thereby resulting in the change in catalytic volume that eventually lead to altered substrate pose. The proximity of substrate (electrophilic C1 of hexose ring) towards the enzyme (O2 of ASP139) is inconsistent for the mutant as compared to native enzyme resulting in less favourable binding energy of substrate. The mutants has detrimental effects contributing to the pathogenesis of the disease	Homo sapiens
R329Q	less favourable binding energy compared to native enzyme. The mutant enzyme possesses reduced volume in the catalytic cleft as compared to native enzyme resulting in the change in substrate pose. Changes in root mean square fluctuation of residues involved in catalytic activity affects the active site in terms of conformational space, thereby resulting in the change in catalytic volume that eventually lead to altered substrate pose. The proximity of substrate (electrophilic C1 of hexose ring) towards the enzyme (O2 of ASP139) is inconsistent for the mutant as compared to native enzyme resulting in less favourable binding energy of substrate. The mutants has detrimental effects contributing to the pathogenesis of the disease	Homo sapiens
R329W	less favourable binding energy compared to native enzyme. The mutant enzyme possesses reduced volume in the catalytic cleft as compared to native enzyme resulting in the change in substrate pose. Changes in root mean square fluctuation of residues involved in catalytic activity affects the active site in terms of conformational space, thereby resulting in the change in catalytic volume that eventually lead to altered substrate pose. The proximity of substrate (electrophilic C1 of hexose ring) towards the enzyme (O2 of ASP139) is inconsistent for the mutant as compared to native enzyme resulting in less favourable binding energy of substrate. The mutants has detrimental effects contributing to the pathogenesis of the disease	Homo sapiens
S160C	less favourable binding energy compared to native enzyme. The mutant enzyme possesses reduced volume in the catalytic cleft as compared to native enzyme resulting in the change in substrate pose. Changes in root mean square fluctuation of residues involved in catalytic activity affects the active site in terms of conformational space, thereby resulting in the change in catalytic volume that eventually lead to altered substrate pose. The proximity of substrate (electrophilic C1 of hexose ring) towards the enzyme (O2 of ASP139) is inconsistent for the mutant as compared to native enzyme resulting in less favourable binding energy of substrate. The mutants has detrimental effects contributing to the pathogenesis of the disease	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P17050	-	-

Synonyms

Synonyms	Comment	Organism
alpha-NAGA	-	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	Schindler disease is a lysosomal storage disorder caused due to deficiency or defective activity of alpha-N-acetylgalactosaminidase	Homo sapiens

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Release 2023.1 (January 2023)