Pathways & interactions
Literature: Alkylmercury lyase (IPR004927)
References used in this entry
The following publications were referred to in the abstract:
Identification of three merB genes and characterization of a broad-spectrum mercury resistance module encoded by a class II transposon of Bacillus megaterium strain MB1.
Huang CC, Narita M, Yamagata T, Endo G.
Gene 239 361-6 1999
PMID: 10548738 Related citations
Nucleotide sequence and expression of the organomercurial-resistance determinants from a Pseudomonas K-62 plasmid pMR26.
Kiyono M, Omura T, Inuzuka M, Fujimori H, Pan-Hou H.
Gene 189 151-7 1997
PMID: 9168120 Related citations
The following publications were not referred to in the abstract, but provide useful additional information:
Bacterial organomercurial lyase: overproduction, isolation, and characterization.
Begley TP, Walts AE, Walsh CT.
Biochemistry 25 7186-92 1986
PMID: 3542021 Related citations
NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyase involved in the bacterial mercury resistance system.
Di Lello P, Benison GC, Valafar H, Pitts KE, Summers AO, Legault P, Omichinski JG.
Biochemistry 43 8322-32 2004
PMID: 15222745 Related citations
Bacterial resistances to inorganic mercury salts and organomercurials.
Plasmid 27 4-16 1992
PMID: 1311113 Related citations
1H, 15N, and 13C resonance assignment of the 23 kDa organomercurial lyase MerB in its free and mercury-bound forms.
Di Lello P, Benison GC, Omichinski JG, Legault P.
J. Biomol. NMR 29 457-8 2004
PMID: 15213467 Related citations
The genetics and biochemistry of mercury resistance.
Crit. Rev. Microbiol. 15 117-40 1987
PMID: 2827958 Related citations