Acetate → 6-Amino-2-oxohexanoic acid

HRID 224911

Reaction equation

HRID 224911 reaction equation
P([O-])([O-])([O-])=O.[K+].[K+].[K+].N[C@H:10]([C:16]([OH:18])=[O:17])[CH2:11][CH2:12][CH2:13][CH2:14][NH2:15].C([O-])(=[O:21])C.Cl.CN1C2C=CC=CC=2SC1=NN>>[O:21]=[C:10]([CH2:11][CH2:12][CH2:13][CH2:14][NH2:15])[C:16]([OH:18])=[O:17]

Participants

5

Procedure

The activity of the present enzyme was measured in accordance with Soda's method (Analytical Biochemistry Vol. 25, p. 228, 1968) in the following manner. A reaction mixture consisting of 0.7 ml of 0.1 M potassium phosphate buffer (pH 8.0), 0.1 ml of catalase (750 U/ml), 0.1 ml of 0.1 M L-lysine solution and 0.1 ml of the present enzyme solution was incubated at 37° C. for 20 minutes with gentle shaking. After the incubation the reaction was terminated by the addition of 0.1 ml of 25% trichloroacetic acid. To the resulting reaction mixture were added 1.9 ml of 1 M acetate buffer (pH 5.0) and 0.8 ml of 0.1% 3-methyl-2-benzothiazolone hydrazone hydrochloride solution. The mixture was further incubated at 30° C. for 30 minutes and then allowed to cool to room temperature, after which measurement of optical density at 318 nm was carried out. The formed α-keto-ε -aminocaproic acid thus formed was determined from the resulting calibration curve. One unit of the enzyme was defined as the quantity of the enzyme catalyzing the formation of 1 μmol of α-keto-ε-aminocaproic acid at 37° C. per minute. The relative activity of the enzyme was also assayed by manometric and polarographic determination of the oxygen consumption.

Workup

  1. customAfter the incubation the reaction was terminated by the addition of 0.1 ml of 25% trichloroacetic acid
  2. customTo the resulting reaction mixture
  3. waitThe mixture was further incubated at 30° C. for 30 minutes

Sources & evidence

ORD record
ord-cf1a7cc260784b448642a5e80cbf8003
Source dataset
uspto-grants-1980_11
Patent number
US04234691

Linked notes

Loading…