Molecular analysis of the Rhodococcus sp. strain H1 her gene and characterization of its product, a heroin esterase, expressed in Escherichia coli.
The structural gene for heroin esterase was cloned from Rhodococcus sp. strain H1 and expressed in Escherichia coli BL21(DE3). The purified enzyme was found to be a tetramer with an M(r) of 137,000 and an apparent K(m) of 0.88 mM for 6-acetylmorphine. The G-x-S-x-G motif was observed in the deduced amino acid sequence, suggesting that the enzyme is a serin esterase.
Rathbone
D A
DA
Institute of Biotechnology, University of Cambridge, United Kingdom.
Holt
P J
PJ
Lowe
C R
CR
Bruce
N C
NC
D000115:Acetylesterase / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D004950:Esterases / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial; D008969:Molecular Sequence Data; D010957:Plasmids; D012240:Rhodococcus / Q000235:genetics*; D017386:Sequence Homology, Amino Acid
D004950:Esterases; C022635:serine esterase; C090778:heroin esterase; D000115:Acetylesterase