General description
Maltose 1-epimerase (MER), is an enzyme that catalyzes the interconversion of α and β anomers of maltose.
Application
Maltose epimerase has been used in a study to assess metabolite gene regulation. It has also been used in a study to investigate saccharogenic determination of α-amylase in serum and urine.
Biochem/physiol Actions
Determination of α-amylase in clinical analysis. Suitable for the determination of maltose.
Other Notes
Enzymatically converts β-maltose to α-maltose.
One unit is defined as the amount of enzyme which converts 1 umol of β-maltose to α-maltose per minute at 25°C and pH 7.0.
Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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L van Leeuwen
Clinical chemistry, 25(2), 215-217 (1979-02-01)
I describe a new kinetic enzymatic saccharogenic method for assaying alpha-amylase in human serum and urine. alpha-Amylase liberates maltose from starch. This is successively acted on by alpha-glucosidase, mutarotase, and glucose dehydrogenase. The resulting conversion of NAD+ to NADH, measured
E L Kline et al.
Journal of bacteriology, 141(2), 770-778 (1980-02-01)
Imidazole, histidine, histamine, histidinol phosphate, urocanic acid, or imidazolepropionic acid were shown to induce the L-arabinose operon in the absence of cyclic adenosine 3',5'-monophosphate. Induction was quantitated by measuring the increased differential rate of synthesis of L-arabinose isomerase in Escherichia
Y Shirokane et al.
Carbohydrate research, 329(3), 699-702 (2000-12-29)
A novel enzymic determination of maltose with four enzymes (a new enzyme, maltose 1-epimerase [EC 5.1.3.-], maltose phosphorylase [EC 2.4.1.8], beta-phosphoglucomutase [EC 5.4.2.6], and glucose-6-phosphate dehydrogenase [EC 1.1.1.49]) is described. Maltose was rapidly and quantitatively determined within about 2 min
Y Shirokane et al.
FEBS letters, 367(2), 177-179 (1995-06-26)
A novel enzyme, maltose 1-epimerase (MER), that catalyzes the interconversion of alpha and beta anomers of maltose was found in a cell-free extract of Lactobacillus brevis IFO 3345, and MER was purified to homogeneity from the crude extract. The M(r)
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