Literature summary for 3.2.1.1 extracted from

Li, C.; Begum, A.; Numao, S.; Park, K.H.; Withers, S.G.; Brayer, G.D.
Acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic alpha-amylase in complex with analogues and their elongated counterparts (2005), Biochemistry, 44, 3347-3357.

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant wild-type pancreatic enzyme, in complex with inhibitors acarbose, isoacarbose, or acarviosine-glucose, hanging drop vapour diffusion method, 0.005 ml of protein solution containing 16.3 mg/ml protein is mixed with 0.005 ml of reservoir solution containing 60% 2-methyl-2,4-pentanediol and 100 mM cacodylate, pH 7.5, 1 month, X-ray diffraction structure determination and analysis at 1.9-2.2 A resolution	Homo sapiens

Crystallization (Comment)

Organism

purified recombinant wild-type pancreatic enzyme, in complex with inhibitors acarbose, isoacarbose, or acarviosine-glucose, hanging drop vapour diffusion method, 0.005 ml of protein solution containing 16.3 mg/ml protein is mixed with 0.005 ml of reservoir solution containing 60% 2-methyl-2,4-pentanediol and 100 mM cacodylate, pH 7.5, 1 month, X-ray diffraction structure determination and analysis at 1.9-2.2 A resolution

Homo sapiens

Inhibitors

Inhibitors	Comment	Organism
acarbose	binding mechanism, acarbose rearrangement mechanism implied by the kinetic and structural analysis, and potential pathways of rearrangement, enzyme-inhibitor complex crystal structure analysis	Homo sapiens
acarviosine-glucose	binding mechanism, resistance to rearrangement, enzyme-inhibitor complex crystal structure analysis	Homo sapiens
isoacarbose	binding mechanism, resistance to rearrangement, enzyme-inhibitor complex crystal structure analysis, binding highly perturbs catalytic residue D300	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P04746	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose	the active site structure involves the catalytic residues D197, E233, and D300, reaction mechanism	Homo sapiens	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
pancreas	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2-chloro-4-nitrophenyl alpha-D-maltotrioside + H2O	-	Homo sapiens	?	-	?
alpha-maltotriosyl fluoride + H2O	-	Homo sapiens	maltotriose + fluoride	-	?
maltosyl fluoride + H2O	-	Homo sapiens	maltose + fluoride	-	?

Synonyms

Synonyms	Comment	Organism
HPA	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
2.98	-	2-chloro-4-nitrophenyl alpha-D-maltotrioside	pH 7.0, 30°C	Homo sapiens
150	-	maltosyl fluoride	pH 7.0, 30°C	Homo sapiens
285	-	alpha-maltotriosyl fluoride	pH 7.0, 30°C	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Homo sapiens