(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Actinobacteria [phylum]: NE > Actinobacteria [class]: NE > Corynebacteriales: NE > Mycobacteriaceae: NE > Mycobacterium: NE > Mycobacterium tuberculosis complex: NE > Mycobacterium tuberculosis: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Mycobacterium tuberculosis TKK-01-0051: N, E.
Mycobacterium tuberculosis EAS054: N, E.
Mycobacterium tuberculosis F11: N, E.
Mycobacterium tuberculosis KZN 1435: N, E.
Mycobacterium tuberculosis H37Ra: N, E.
Mycobacterium tuberculosis T17: N, E.
Mycobacterium tuberculosis T85: N, E.
Mycobacterium tuberculosis 94_M4241A: N, E.
Mycobacterium tuberculosis 02_1987: N, E.
Mycobacterium tuberculosis T46: N, E.
Mycobacterium tuberculosis C: N, E.
Mycobacterium tuberculosis GM 1503: N, E.
Mycobacterium tuberculosis CPHL_A: N, E.
Mycobacterium tuberculosis K85: N, E.
Mycobacterium tuberculosis CDC1551: N, E.
Mycobacterium tuberculosis SUMu011: N, E.
Mycobacterium tuberculosis SUMu010: N, E.
Mycobacterium tuberculosis SUMu009: N, E.
Mycobacterium tuberculosis SUMu008: N, E.
Mycobacterium tuberculosis SUMu007: N, E.
Mycobacterium tuberculosis SUMu006: N, E.
Mycobacterium tuberculosis SUMu003: N, E.
Mycobacterium tuberculosis SUMu012: N, E.
Mycobacterium tuberculosis SUMu005: N, E.
Mycobacterium tuberculosis SUMu004: N, E.
Mycobacterium tuberculosis SUMu002: N, E.
Mycobacterium tuberculosis SUMu001: N, E.
Mycobacterium tuberculosis str. Haarlem: N, E.
Mycobacterium tuberculosis T92: N, E.
Mycobacterium tuberculosis str. Erdman = ATCC 35801: N, E.
Mycobacterium tuberculosis FJ05194: N, E.
Mycobacterium tuberculosis EAI5/NITR206: N, E.
Mycobacterium tuberculosis UT205: N, E.
Mycobacterium tuberculosis CCDC5180: N, E.
Mycobacterium tuberculosis H37Rv: N, E.
Mycobacterium tuberculosis CDC1551A: N, E.
Mycobacterium tuberculosis CCDC5079: N, E.
Mycobacterium tuberculosis BT2: N, E.
Mycobacterium tuberculosis EAI5: N, E.
Mycobacterium tuberculosis W-148: N, E.
Mycobacterium tuberculosis CTRI-2: N, E.
Mycobacterium tuberculosis RGTB327: N, E.
Mycobacterium tuberculosis str. Haarlem/NITR202: N, E.
Mycobacterium tuberculosis '98-R604 INH-RIF-EM': N, E.
Mycobacterium tuberculosis str. Beijing/NITR203: N, E.
Mycobacterium tuberculosis HKBS1: N, E.
Mycobacterium tuberculosis CAS/NITR204: N, E.
Mycobacterium tuberculosis 7199-99: N, E.
Mycobacterium tuberculosis KZN 605: N, E.
Mycobacterium tuberculosis NCGM2209: N, E.
Mycobacterium tuberculosis BT1: N, E.
Mycobacterium tuberculosis RGTB423: N, E.
Mycobacterium tuberculosis KZN 4207: N, E.
Mycobacterium tuberculosis GuangZ0019: N, E.
Mycobacterium tuberculosis 2092HD: N, E.
Mycobacterium tuberculosis variant caprae: N, E.
Mycobacterium tuberculosis variant africanum: N, E.
Mycobacterium tuberculosis variant microti OV254: N, E.
Molecular evidence
Database
No mutation 1 structure: 7C72: Structure of a mycobacterium tuberculosis puromycin-hydrolyzing peptidase No kinetic
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MTARATLPYGSWPSPISAADVARARLRLSFPTVAGDDVWWQETRPEEDGR TTVIHLRGGHRTELLQAPWDARTRVHEYGGRSYLPIRTAEGWSVVFSNYD DQRLHRLDEGDPKPYPLTPLPAVPAGLRYADYVLSPDGTEVWCVCEGHIA APPEPPPAEGEEGAPASEEPAVTGIRRAIVAIPLDGRAAEDAGAIRELVA GAQFYASPAPSPGGGHLAWVQWNHPRMPWDGTEVRVAAVEDGRTVAPRTV KGGLKESALAPLWRDEESLYVISDWPGWWNIYQVGLHGESPQALYPAEEE FAGPLWQLGGMPYALLGDGRLAVLHGEGDLRLGVYDPETLDLVDLEVPYE HWATQLSADGTTVVGIGGGPDLPASVVRVDTTTGRVEGLRRELAELPNVA YLSRPRAERLDGPFGRPVHAYVFPPTNPEAAAPEGELPPYVVFVHGGPTG RVSTVLDLERVYFTSRGIGVIDVNYGGSTGYGRAYRERLRRQWGVVDVED AIAAAQALVDGGIADPARLAIRGGSAGGWTTLAAITQTDVFKAATSYFGI SDLQSFAEATHDFESQYLFGLIGPLPGFERAYEERSPLRHADRTACPVLL LQGLNDPVVPPDQSERFALALADKKMPYAYLTFEGESHGFRKAGTVVRSL EAELAFYGQTLGFEPRGVEPINLTVG
Puromycin-hydrolizing peptidases have been described as members of the prolyl oligopeptidase peptidase family. These enzymes are present across all domains of life but still little is known of the homologs found in the pathogenic bacterium Mycobacterium tuberculosis. The crystal structure of a M. tuberculosis puromycin hydrolase peptidase has been determined at 3 Angstrom resolution, revealing a conserved prolyl oligopeptidase fold, defined by alpha/beta-hydrolase and beta-propeller domains with two distinctive loops that occlude access of large substrates to the active site. The enzyme displayed amino peptidase activity with a substrate specificity preference for hydrophobic residues in the decreasing order of phenylalanine, leucine, alanine and proline. The enzyme's active site is lined by residues Glu564 for the coordination of the substrates amino terminal moiety and His561, Val608, Tyr78, Trp306, Phe563 and Ty567 for the accommodation of hydrophobic substrates. The availability of a crystal structure for puromycin hydrolase of M. tuberculosis shall facilitate the development of inhibitors with therapeutic applications. This article is protected by copyright. All rights reserved.
Mycobacterium tuberculosis Puromycine hydrolase
