Identification of a heroin esterase in Rhodococcus sp. strain H1.
A strain of a Rhodococcus sp. (termed H1) capable of utilizing heroin as its sole carbon and energy source was isolated by selective enrichment. An inducible heroin esterase was partially purified and shown to catalyze the hydrolysis of both of the acetylester groups of heroin. The enzyme displays optimum activity at pH 8.5 and appears to be a trimer of identical subunits with an M(r) or 39,000 and a native M(r) of 120,000.
Cameron
G W
GW
Institute of Biotechnology, University of Cambridge, United Kingdom.
Jordan
K N
KN
Holt
P J
PJ
Baker
P B
PB
Lowe
C R
CR
Bruce
N C
NC
D000115:Acetylesterase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D003932:Heroin / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011487:Protein Conformation; D012240:Rhodococcus / Q000201:enzymology* / Q000235:genetics
D003932:Heroin; C090778:heroin esterase; D000115:Acetylesterase