MalL

• Description: alpha-glucosidase
  
  

Gene name	malL
Synonyms	yvdL
Essential	no
Product	alpha-glucosidase
Function	starch and maltodextrin utilization
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism, Sugar catabolism
MW, pI	65 kDa, 4.98
Gene length, protein length	1683 bp, 561 aa
Immediate neighbours	pgcM, yvdK
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

utilization of specific carbon sources

The gene

Basic information

• Locus tag: BSU34560

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose (according to Swiss-Prot)

• Protein family: glycosyl hydrolase 13 family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 1UOK (from Bacillus cereus, 57% identity, 74% similarity) PubMed

• UniProt: O06994

• KEGG entry: [2]

• E.C. number: 3.2.1.10

Expression and regulation

• Operon: yvdE-yvdF-mdxE-mdxF-mdxG-yvdJ-yvdK-malL-pgcM PubMed

• Expression browser: malL PubMed

• Sigma factor:

• Regulation:
  • induced in the presence of maltose PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Stefan Schönert, Sabine Seitz, Holger Krafft, Eva-Anne Feuerbaum, Iris Andernach, Gabriele Witz, Michael K Dahl
Maltose and maltodextrin utilization by Bacillus subtilis.
J Bacteriol: 2006, 188(11);3911-22
[PubMed:16707683] [WorldCat.org] [DOI] (P p)

S Schönert, T Buder, M K Dahl
Properties of maltose-inducible alpha-glucosidase MalL (sucrase-isomaltase-maltase) in Bacillus subtilis: evidence for its contribution to maltodextrin utilization.
Res Microbiol: 1999, 150(3);167-77
[PubMed:10229946] [WorldCat.org] [DOI] (P p)

S Schönert, T Buder, M K Dahl
Identification and enzymatic characterization of the maltose-inducible alpha-glucosidase MalL (sucrase-isomaltase-maltase) of Bacillus subtilis.
J Bacteriol: 1998, 180(9);2574-8
[PubMed:9573215] [WorldCat.org] [DOI] (P p)