Enzymatic Synthesis of 12-Aminolauric Acid
2149
2
5)
anoate-cyclic-dimer hydrolase (EI),
5)
6-aminohexa-
noate-dimer hydrolase (EII), and endo-type 6-amino-
Identification and characterization of aliphatic amidase
in Helicobacter pylori. Mol. Microbiol., 25, 989–998
(1997).
3
3
6)
hexanoate-oligomer hydrolase (EIII), and the respon-
sible genes are encoded on plasmid pOAD2 (45,519 bp)
1
1) Cheong, T. K., and Oriel, P. J., Cloning of a wide-
spectrum amidase from Bacillus stearothermophilus
BR388 in Escherichia coli and marked enhancement of
amidase expression using directed evolution. Enzyme
Microb. Technol., 26, 152–158 (2000).
2) Fernandez-Lafuente, R., Rosell, C. M., and Guisan,
J. M., Enzyme reaction engineering: synthesis of anti-
biotics catalyzed by stabilized penicillin G acylase in the
presence of organic solvents. Enzyme Microb. Technol.,
13, 898–905 (1991).
3) Wakayama, M., Yoshimune, K., Hirose, Y., and
Moriguchi, M., Production of D-amino acids by N-
acyl-D-amino acid amidehydrolase and its structure and
function. J. Mol. Cat. B: Enzymatic, 23, 71–85 (2003).
4) Asano, Y., Nakazawa, A., Kato, Y., and Kondo, K.,
Properties of a novel D-stereospecific aminopeptidase
from Ochrobactrum anthropi. J. Biol. Chem., 264,
3
7)
in Arthrobacter KI72. The gene encoding !-laurolac-
tam hydrolase was cloned from the genomic DNA of
Rhodococcus sp. U224. A plasmid extraction from the
strain U224 was tried, but no any plasmids such as
pOAD2 were detected in the strain. It is not clear
whether the gene encoding !-laurolactam hydrolase is
isolated on the genomic DNA or the plasmid DNA. On
the other hand, 6-aminohexanoate-cyclic-dimer hydro-
lase was found to be an inducible enzyme from the
observation that the cell extract did not hydrolyze the
cyclic dimer when the cells were harvested from nutrient
broth without the cyclic dimer. However, all !-laur-
olactam degrading microorganisms hydrolyzed !-laur-
olactam when the cells were harvested from nutrient
broth with or without !-laurolactam. This suggests that
-laurolactam hydrolase is a constitutive enzyme.
Hydrolysis of !-laurolactam by microorganisms has
never before been reported. This study suggests that the
microorganisms screened can perhaps be used effec-
tively in the production of 12-aminolauric acid from
-laurolactam, since it is difficult to prepare it by
chemical reaction. A possible mechanism by which an
enzyme is active towards synthetic substances such as
1
1
1
1
1
1
4233–14239 (1989).
!
5) Asano, Y., Ito, H., Dairi, T., and Kato, Y., An alkaline
D-stereospecific endopeptidase with ꢀ-lactamase activity
from Bacillus cereus. J. Biol. Chem., 271, 30256–30262
(1996).
6) Komeda, H., and Asano, Y., Gene cloning, nucleotide
sequencing, and purification and characterization of the
D-stereospecific amino acid amidase from Ochrobactrum
anthropi SV3. Eur. J. Biochem., 267, 2028–2036 (2000).
7) Livermore, M. D., ꢀ-Lactamases in the laboratory and
clinical resistance. Clin. Microbiol. Rev., 8, 557–584
!
1
1
!
-laurolactam is that a non-natural compound is hydro-
lyzed as an analogue of a physiological substrate, but
this is not clear.
(
1995).
8) Taylor, S. J. C., McCague, R., Wisdom, R., Lee, C.,
Dickson, K., Ruecroft, G., O’Brien, F., Littlechild, J.,
Bevan, J., Roberts, S. M., and Evans, C. T., Develop-
ment of the biocatalytic resolution of 2-azabicy-
clo[2.2.1]-hept-5-en-3-one as an entry to single enan-
tiomer carbocyclic nucleosides. Tetrahedron Assym., 4,
1117–1128 (1993).
19) Brabban, A. D., Littlechild, J. A., and Wisdom, R.,
Stereospecific ꢁ-lactamase activity on Pseudomonas
fluorescens sp. J. Ind. Microbiol., 16, 8–14 (1996).
20) Taylor, S. J. C., Brown, R. C., Keene, P. A., and Taylor,
I. N., Novel screening methods: the key to cloning
commercially successful biocatalysis. Bioorg. Med.
Chem., 7, 2163–2168 (1999).
21) Line, K., Isupov, M., and Littlechild, J., The crystal
structure of a (ꢃ) ꢁ-lactamase from an Aureobacterium
sp. reveals a tetrahedral intermediate in the active site.
J. Mol. Biol., 338, 519–532 (2004).
22) Fukumura, T., Hydrolysis of L-ꢂ-amino-"-caprolactam
by yeasts. Agric. Biol. Chem., 40, 1695–1698 (1976).
23) Fukumura, T., Talbot, G., Misono, H., Teramura, Y.,
Kato, K., and Soda, K., Purification and properties of
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1