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4-alpha-Glucanotransferase

Known as: dextrin glycosyl-transferase, disproportionating enzyme, amylomaltase 
National Institutes of Health

Related topics

Related topics

2 relations
Glucosyltransferase

Broader (1)

Glycogen Debranching Enzyme System

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2009
Highly Cited
2009
Fine structural properties of natural and synthetic glycogens.
Highly Cited
1999
Highly Cited
1999
Purification and properties of a novel raw starch degrading cyclomaltodextrin glucanotransferase from Bacillus firmus
Abstract A novel raw starch degrading cyclomaltodextrin glucanotransferase (CGTase; E.C. 2.4.1.19), produced by Bacillus firmus… 
Highly Cited
1992
Highly Cited
1992
Characterization of carbohydrate metabolism and demonstration of glycosomes in a Phytomonas sp. isolated from Euphorbia characias.
1990
1990
Effects of modifications at the C-terminus of cyclomaltodextrin glucanotransferase from Bacillus circulans var. alkalophilus on catalytic activity
Highly Cited
1988
Highly Cited
1988
Molecular characterization of malQ, the structural gene for the Escherichia coli enzyme amylomaltase
The structural gene for the Escherichia coli enzyme amylomaltase, malQ, is the second gene in the malPQ operon. The nucleotide… 
Highly Cited
1985
Highly Cited
1985
A convenient technique to compare the efficiency of promoters in Escherichia coli.
We describe a technique which allows one to insert any promoter in front of the chromosomal malPQ operon. This can be done easily… 
Highly Cited
1980
Highly Cited
1980
Catabolite repression in Escherichia coli mutants lacking cyclic AMP receptor protein.
Pleiotropic carbohydrate-positive pseudorevertants have been isolated from a specific class of rho-crp double mutants of… 
Highly Cited
1960
Highly Cited
1960
The characterization of the pathway of maltose utilization by Escherichia coli. I. Purification and physical chemical properties of the enzyme amylomaltase.
Highly Cited
1960
Highly Cited
1960
The characterization of the pathway of maltose utilization by Escherichia coli. II. General properties and mechanism of action of amylomaltase.
Highly Cited
1952
Highly Cited
1952
Phosphorolysis of maltose by enzyme preparations from Neisseria meningitidis.
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