Family M81


Summary Holotypes Alignment Tree Genomes Structure Literature Architecture

Summary for family M81

Family type peptidaseM81.001 - microcystinase MlrC (Sphingomonas sp. ACM-3962), MEROPS Accession MER0167712 (peptidase unit: 1-325)
Content of familyPeptidase family M81 contains metallopeptidases.
History Identifier created: MEROPS 9.4 (31 January 2011)
Microcystins are peptide toxins produced by cyanobacteria which can cause hepatotoxicity by inhibiting protein phosphatases. Microcystins are heptapeptides containing unusual amino acids. Microcystin LR (cyclo(NH2-Adda-isoGlu-methyldehydroAla-Leu-beta-methylAsp-Arg)) is one of the commonest microcystins, persisting in contaminated water supplies for weeks. Efforts to find a method to remove the microcystin led to the discovery of a species of Sphingomonas which can utilize the microcystin as a source of carbon and nitrogen. The bacterium has three specialized peptidase to degrade it. Microcystinase (G05.004) converts the cyclic peptide to a linear peptide, MlrB peptidase (S12.009) cleaves the methyldehydroAla-Leu bond to generate two fragments (Bourne et al., 1996), and the tetrapeptide is further degraded by the MlrC peptidase (M81.001; Bourne et al., 2001) but the exact cleavage position is unknown.
Catalytic typeMetallo
Active siteFrom the deduced crystal structure of a homologue from Mesorhizobium sp. BNC1, a single zinc ion is bound by Asp38, His140 and His162. The histidines are well conserved, but the aspartic acid is not.
Activities and specificitiesThe MlrC peptidase from Sphingopyxis degrades both microcystins LR and LA (Ho et al., 2007).
InhibitorsThe MlrC peptidase is assumed to be a metallopeptidase because of inhibition by metal chelators (Bourne et al., 2001).
Molecular structureThe tertiary structure has been solved for a biochemically uncharacterized homologue from Mesorhizobium sp. BNC1. The structure has been deposited in the Protein Data Bank but has not yet been published. The structure show a two-domain protein, with each domain containing a beta sheet surrounded by helices. The active site containing the zinc ion is between the domains. The fold is unlike that of any other peptidase, but related to ABC ribose transporters, alanine racemase, maltose operon transcriptional repressors, and chemotaxis protein Chey. Consequently, the structure of the Mesorhizobium homologue is the type structure for clan MT.
Distribution of family Bacteria details  
Archaea details  
Protozoa -  
Fungi -  
Plants -  
Animals details  
Viruses -  
Biological functionsThe genes for the three microcystin-degrading peptidases and a putative oligopeptide transporter are found in the same 5.8 kilobase genomic fragment (Bourne et al., 2001).
Statistics for family M81Sequences:548
Identifiers with PDB entries:1
Downloadable files Sequence library (FastA format)
Sequence alignment (FastA format)
Phylogenetic tree (Newick format)
Other databases INTERPRO IPR015995
PFAM PF07171
PFAM PF07364
Peptidases and Homologues MEROPS ID Structure
microcystinase MlrCM81.001-
Family M81 unassigned peptidasesunassignedYes