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MGAM, or nearby regulatory elements, may be involved in the etiology of oral clefts.
Starch internal structure modulates its susceptibility to MGAM. The internal branch amounts negatively affect the glucose release rate.
The over-expression of MGAM was confirmed with a 6.6 fold increase in expression at the mRNA level whereas the fold change in ADAM9 (zeige ADAM9 Proteine) demonstrated a 1.6 fold increase.
Findings suggest that C-terminal subunits of recombinant maltase-glucoamylase (MGAM) assists alpha-amylase (zeige AMY Proteine) in digesting starch molecules and potentially may compensate for developmental or pathological amylase (zeige AMY Proteine) deficiencies.
These results suggest that the N-terminal and C-terminal catalytic domains of maltase-glucoamylase differ in their substrate specificities and inhibitor tolerance despite their structural relationship
we report crystal structures of C-terminal maltase-glucoamylase alone at a resolution of 3.1 angstroms, and in complex with its inhibitor acarbose
analysis of substrate selectivity of human maltase-glucoamylase and sucrase-isomaltase N-terminal domains
genetic analysis of MGAM, exon boundaries, and chromosome mapping
Raw starch granule degradation with recombinanat human MGAM indicates that pancreatic alpha-amylase (zeige AMY2A Proteine) hydrolysis is not a requirement for native starch digestion in the human small intestine.
Intestinal maltase-glycoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
Core2 O-glycan structure is essential for expression of SI and DDP (zeige TIMM8A Proteine)-IV during intestinal cell differentiation.
These suggest that induction of SI gene by the diet rich in carbohydrate is associated with acetylation of histone H3 (zeige HIST3H3 Proteine) and H4 as well as binding of HNF-1 (zeige HNF1A Proteine) and Cdx-2 (zeige CDX2 Proteine) on SI gene.
This gene encodes maltase-glucoamylase, which is a brush border membrane enzyme that plays a role in the final steps of digestion of starch. The protein has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities.
alpha glucosidase 2
, acid (Pompe disease, glycogen storage disease type II)
, acid alpha-glucosidase
, acid maltase
, glucosidase, alpha; acid (Pompe disease, glycogen storage disease type II)
, lysosomal alpha-glucosidase
, brush border hydrolase
, maltase-glucoamylase, intestinal
, sucrase isomaltase, structural
, sucrase-isomaltase, intestinal