Potassium Chloride → Deacetoxycephalosporin C

HRID 1090609Notes

Reaction equation

HRID 1090609 reaction equation
[CH3:1][C:2]1([CH3:24])[S:6][C@@H:5]2[C@H:7]([NH:10][C:11]([CH2:13][CH2:14][CH2:15][C@@H:16]([NH2:20])[C:17]([OH:19])=[O:18])=[O:12])[C:8](=[O:9])[N:4]2[C@H:3]1[C:21]([OH:23])=[O:22].[Cl-].[K+]>OCC(CO)O>[CH3:1][C:2]1[CH2:24][S:6][C@@H:5]2[C@H:7]([NH:10][C:11]([CH2:13][CH2:14][CH2:15][C@@H:16]([NH2:20])[C:17]([OH:19])=[O:18])=[O:12])[C:8](=[O:9])[N:4]2[C:3]=1[C:21]([OH:23])=[O:22]

Participants

4

Reactant 2

HCID 4873Potassium ChlorideHCID 71724(4-Amino-4-carboxybutyl)penicillin

Product 1

HCID 160139Deacetoxycephalosporin C

Reagents, catalysts & solvents 1

HCID 753GlycerolSolvent

Procedure

The fractions containing 80% of the enzyme activity from the major peak were pooled. The pooled fractions were supplemented with 0.1 mM penicillin N and were loaded onto a second Mono Q column (0.5×5 cm) which had been equilibrated with the glycerol-free buffer, pH 7.0, (instead of pH 8.0 for UDG buffer), which was supplemented with 0.05 M KCl. The bound proteins were eluted with a linear gradient of KCl 0.05-0.2 M) in the equilibration buffer. The activity and protein elution patterns are shown in FIG. 4A. The three fractions with a synthase activity of at least 275 mU/ml were pooled.

Workup

  1. additionThe fractions containing 80% of the enzyme activity from the major peak
  2. washThe bound proteins were eluted with a linear gradient of KCl 0.05-0.2 M) in the equilibration buffer
  3. washThe activity and protein elution patterns

Sources & evidence

ORD record
ord-81343931013f44109db14e8b44a3565f
Source dataset
uspto-grants-1992_01
Patent number
US05082772

Reaction notes

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