This is the catalytic region of aspzincins, a group of lysine-specific metallo-endopeptidases in the M35 family. They exhibit the following active-site architecture. The active site is composed of two helices and a loop region and includes the HExxH and GTxDxxYG motifs. In UniProt:P81054 His117, His121 and Asp130 coordinate to the catalytic zinc ligands. An electrostatically negative region composed of Asp154 and Glu157 attracts a positively charged Lys side chain of a substrate in a specific manner (PMID:11679721).
This is the catalytic domain of aspzincins, a group of lysine-specific metallo-endopeptidases in the MEROPS M35 family. They exhibit the following active-site architecture: the active site is composed of two helices and a loop region and includes the HExxH and GTxDxxYG motifs. In protein P81054 His117, His121 and Asp130 coordinate to the catalytic zinc ligands. An electrostatically negative region composed of Asp154 and Glu157 attracts a positively charged Lys side chain of a substrate in a specific manner [ (PUBMED:11223512) ].
There are 911 Aspzincin_M35 domains in 911 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing Aspzincin_M35 domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Aspzincin_M35 domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing Aspzincin_M35 domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
A quick solution: ab initio structure determination of a 19 kDa metalloproteinaseusing ACORN.
Acta Crystallogr D Biol Crystallogr. 2001; 57: 1571-8
Display abstract
A data set from the metalloproteinase deuterolysin was collected at atomicresolution (1.0 A) with synchrotron radiation. The high resolution allowed thestructure to be solved with the new direct-methods program ACORN using thecoordinates of the Zn atom as a starting point. The phases obtained from ACORNwere of sufficient quality to allow automated building to be carried out inARP/wARP. Minimal manual rebuilding of the model was required and the structuredetermination was completed using the maximum-likelihood refinement programREFMAC. The whole process, starting from the processed and merged data and endingwith a refined model, required less than 6 h of computational time.
Kinetic characterization of lysine-specific metalloendopeptidases from Grifolafrondosa and Pleurotus ostreatus fruiting bodies.
J Biochem. 1998; 124: 157-62
Display abstract
Two zinc-metalloendopeptidases, GFMEP (accession number P81054) and POMEP(accession number P81055), from the fruiting bodies of two edible mushrooms,Grifola frondosa and Pleurotus ostreatus, respectively, specifically hydrolyzepeptidyl-lysine bonds (-X-Lys-) in polypeptides. To understand detailed substratespecificities and kinetic characters of these enzymes, we have synthesizedvarious intramolecularly quenched fluorescent peptide substrates and determinedtheir kinetic constants with these substrates. Each synthesized fluorogenicpeptide has a fluorescent residue, tryptophan, at its carboxyl terminus and aquenching group, dinitrophenyl (Dnp), at its amino terminus. Quenching of the Trpfluorescence in an intact substrate is relieved on hydrolysis of the -X-Lys-bond, giving rise to a continuous increase in fluorescence. The octapeptidesubstrate, Dnp-Ser-Thr-Ala-Thr-Lys-Leu-Ser-Trp, was an efficient substrate forboth enzymes, the kcat/Km values being 9.8 x 10(6) and 7.0 x 10(5) M-1.s-1 forGF- and POMEP, respectively. Peptides with aspartic acid adjacent to the Lysresidue were found to be poor substrates for both enzymes. Neither the shortestpeptide, Dnp-Thr-Lys-Trp, nor peptides with substitution of L-Arg, L-ornithine,or D-Lys for Lys were hydrolyzed by either enzyme. These results confirmed thestrict specificities of GF- and POMEP toward the peptide bond, -X-Lys-.Substitution of Co2+ for Zn2+ enhanced the activity, while the Km values werecomparable. All peptides not hydrolyzed by either enzyme had inhibitory effectson GFMEP activity. The active site structure is discussed in relation to theseobservations.
