Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori.

doi:10.1093/protein/3.3.193

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Article

Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori.

Protein engineering - 1 Jan 1990

Sierks M R, Ford C, Reilly P J, Svensson B

Abstract excerpt

Asp176, Glu179 and Glu180 of Aspergillus awamori glucoamylase appeared by differential labeling to be in the active site. To test their functions, they were replaced by mutagenesis with Asn, Gln and Gln respectively, and kinetic parameters and pH dependencies of all enzyme forms were determined. Glu179----Gln glucoamylase was not active on maltose or isomaltose, while the kcat for maltoheptaose hydrolysis...

Topics

Amino Acid Sequence
Aspartic Acid
Aspergillus
Base Sequence
Binding Sites
Catalysis
DNA Restriction Enzymes
Glucan 1,4-alpha-Glucosidase
Glucans
Glutamates
Glutamic Acid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Hydrogen-Ion Concentration

Isomaltose

Kinetics

Maltose

Molecular Sequence Data

Mutation

Sequence Homology, Nucleic Acid

Source

Open in PubMed

Identifiers

PMID: 1970434
DOI: 10.1093/protein/3.3.193

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1970434-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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