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β-amylase


'β-amylase' can also refer to...

β‐amylase

Water stress enhances β‐amylase activity in cucumber cotyledons

Improvement of Bacillus circulans β-amylase activity attained using the ancestral mutation method

β-amylase 1 (BAM1) degrades transitory starch to sustain proline biosynthesis during drought stress

Interaction of wheat β-amylase with maltose and glucose as examined by fluorescence

Purification and characterization of novel organic-solvent-tolerant β-amylase and serine protease from a newly isolated Salimicrobium halophilum strain LY20

Change in the crystal packing of soybean β‐amylase mutants substituted at a few surface amino acid residues

Evolution of α-Amylases: Architectural Features and Key Residues in the Stabilization of the (β/α)8 Scaffold

Intraspecies differences in cold hardiness, carbohydrate content and β-amylase gene expression of Vaccinium corymbosum during cold acclimation and deacclimation

Two Additional Carbohydrate-Binding Sites of β-Amylase from Bacillus cereus var. mycoides Are Involved in Hydrolysis and Raw Starch-Binding

Thioredoxin-regulated β-amylase (BAM1) triggers diurnal starch degradation in guard cells, and in mesophyll cells under osmotic stress

Crystal Structure of βAmylase from Bacillus cereus var. mycoides at 2.2 Å Resolution

Crystal Structures of β-Amylase from Bacillus cereus var. mycoides in Complexes with Substrate Analogs and Affinity-Labeling Reagents

Catalytic Mechanism of β-Amylase from Bacillus cereus var. mycoides: Chemical Rescue of Hydrolytic Activity for a Catalytic Site Mutant (Glu367→Ala) by Azide

Studies on the Hydrolyzing Mechanism for Cyclodextrins of Thermoactinomyces vulgaris R-47 α-Amylase 2 (TVAII). X-Ray Structure of the Mutant E354A Complexed with β-Cyclodextrin, and Kinetic Analyses on Cyclodextrins

 

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EC 3.2.1.2; systematic name: 1,4‐α‐d‐glucan maltohydrolase; other names: saccharogen amylase; glycogenase. An enzyme that removes successive maltose units from the nonreducing ends of carbohydrate chains; the anomeric group undergoes inversion ...

Subjects: Chemistry.


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