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Literature summary for 3.2.1.1 extracted from

  • Koropatkin, N.M.; Smith, T.J.
    SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules (2010), Structure, 18, 200-215.
    View publication on PubMed
Search for more literature for 3.2.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
SusG D498N mutant with bound maltoheptaose, Ca2+ replaces the Mg2+ ion observed in the apo structure, X-ray diffraction structure determination and analysis at 2.3 A resolution Bacteroides thetaiotaomicron

Protein Variants

Protein Variants Comment Organism
D498N site-directed mutagenesis, a catalytically inactive mutant, crystal structure determination and analysis Bacteroides thetaiotaomicron

Inhibitors

Inhibitors Comment Organism Structure
acarbose a pseudotetrasaccharide inhibitor of alpha-amylase and alpha-glucosidase, binding structure, overview Bacteroides thetaiotaomicron

Localization

Localization Comment Organism GeneOntology No. Textmining
outer membrane
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 Bacteroides thetaiotaomicron 19867
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Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 2 ions per enzyme molecule Bacteroides thetaiotaomicron
Mg2+ 2 ions per enzyme molecule Bacteroides thetaiotaomicron

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
amylopectin + H2O Bacteroides thetaiotaomicron
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 ?
-
 ?
amylose + H2O Bacteroides thetaiotaomicron
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 ?
-
 ?
pullulan + H2O Bacteroides thetaiotaomicron
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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bacteroides thetaiotaomicron Q8A1G3 human gut symbiont
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Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amylopectin + H2O
-
 Bacteroides thetaiotaomicron ?
-
 ?
amylose + H2O
-
 Bacteroides thetaiotaomicron ?
-
 ?
additional information maltooligosaccharide bind to the carbohydrate-binding domain, CBM58, of SusG. SusG is flexible in its carbohydrate selectivity because it binds to and degrades pullulan, amylopectin, and amylose. It shows low activity on alpha- and beta-cyclodextrins Bacteroides thetaiotaomicron ?
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 ?
pullulan + H2O
-
 Bacteroides thetaiotaomicron ?
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 ?

Subunits

Subunits Comment Organism
More SusG is composed of A, B, and C domains that share structural features with other amylases. The A domain, residues 43-152 and 364-607, has an eight-stranded alpha/beta barrel that contains the catalytic site, with the B domain, residues 153-215 and 336-363, inserted between beta3 and alpha3 of the A domain. The B domain consists of two two-stranded antiparallel beta sheets, two alpha helices, and three 310 helices that pack against the A domain and contribute to the size and accessibility of the active site. The C domain, residues 608-692, folds into an eight-stranded beta sandwich, structure model, overview Bacteroides thetaiotaomicron

Synonyms

Synonyms Comment Organism
SusG
-
 Bacteroides thetaiotaomicron

General Information

General Information Comment Organism
additional information determination of the structure of carbohydrate binding CBM58-binding site, the active site, and the surface starch-binding site, directly adjacent to the reducing end of the active site Bacteroides thetaiotaomicron
physiological function SusG is the alpha-amylase expressed concomitantly with Sus-CDEF on the outer surface of the cell and is absolutely required for growth on starch Bacteroides thetaiotaomicron