Thermolysin: Difference between revisions
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* Thermolysin | * Thermolysin | ||
**[[2whz]], [[3fvp]], [[3dnz]], [[3do0]], [[3do1]], [[3do2]], [[2g4z]], [[2a7g]], [[1gxw]], [[1kei]], [[1l3f]], [[1tlx]], [[2tlx]], [[8tln]], [[3p7p]], [[3p7q]], [[3p7r]], [[3p7s]], [[3p7t]], [[3p7u]], [[3p7v]], [[3p7w]], [[3zi6]] – TML<br /> | **[[2whz]], [[3fvp]], [[3dnz]], [[3do0]], [[3do1]], [[3do2]], [[2g4z]], [[2a7g]], [[1gxw]], [[1kei]], [[1l3f]], [[1tlx]], [[2tlx]], [[8tln]], [[3p7p]], [[3p7q]], [[3p7r]], [[3p7s]], [[3p7t]], [[3p7u]], [[3p7v]], [[3p7w]], [[3zi6]], [[5dlh]], [[5tli]], [[6tli]], [[7tli]], [[8tli]], [[5un3]], [[5uu7]], [[5wr2]], [[5wr3]], [[5wr4]], [[5wr5]], [[5wr6]], [[5a3y]], [[5o8n]], [[5uu8]], [[5uu9]], [[5uua]], [[5uub]], [[5uuc]], [[5uud]], [[5uue]], [[5fsj]], [[5fsp]], [[5fss]], [[5fxn]], [[5t9i]], [[5t9k]], [[5t9q]], [[5tac]], [[5tad]], [[5tae]], [[5tai]], [[5taj]], [[5tak]], [[5hqd]] – TML<br /> | ||
**[[5dlh]] – TML - electron crystallography<br /> | |||
**[[3ls7]], [[4ow3]], [[4tnl]] - TML residues 233-548<br /> | **[[3ls7]], [[4ow3]], [[4tnl]] - TML residues 233-548<br /> | ||
**[[1trl]] - TML residues 255-316 – NMR<br /> | **[[1trl]] - TML residues 255-316 – NMR<br /> | ||
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*Thermolysin + dipeptide | *Thermolysin + dipeptide | ||
**[[2wi0]], [[3tmn]] – TML+ dipeptide <br /> | **[[2wi0]], [[3tmn]], [[8tln]] – TML+ dipeptide <br /> | ||
**[[3fgd]] - TML residues 233-548+dipeptide<br /> | **[[3fgd]] - TML residues 233-548+dipeptide<br /> | ||
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**[[1fjo]], [[1fj3]], [[1fjq]], [[1fjt]], [[1fju]], [[1fjv]], [[1fjw]], [[4tli]], [[5tli]], [[6tli]], [[7tli]], [[8tli]], [[1tli]], [[2tli]], [[3tli]] – TML soaked in organic solvents<br /> | **[[1fjo]], [[1fj3]], [[1fjq]], [[1fjt]], [[1fju]], [[1fjv]], [[1fjw]], [[4tli]], [[5tli]], [[6tli]], [[7tli]], [[8tli]], [[1tli]], [[2tli]], [[3tli]] – TML soaked in organic solvents<br /> | ||
**[[3fv4]], [[3fxp]], [[3flf]], [[3fb0]], [[3fcq]], [[3f28]], [[3f2p]], [[4mtw]], [[4mwp]], [[4mxj]], [[4mzn]], [[4n4e]], [[4n5p]], [[4n66]], [[4oi5]] – TML residues 233-548+inhibitor<br /> | **[[3fv4]], [[3fxp]], [[3flf]], [[3fb0]], [[3fcq]], [[3f28]], [[3f2p]], [[4mtw]], [[4mwp]], [[4mxj]], [[4mzn]], [[4n4e]], [[4n5p]], [[4n66]], [[4oi5]] – TML residues 233-548+inhibitor<br /> | ||
**[[3for]], [[1y3g]], [[1zdp]], [[1z9g]], [[1pes]], [[1pe7]], [[1pe8]], [[1os0]], [[1kto]], [[1ks7]], [[1kro]], [[1kr6]], [[1kkk]], [[1kjo]], [[1kjp]], [[1qf0]], [[1qf1]], [[1qf2]], [[1hyt]], [[1thl]], [[6tmn]], [[7tln]], [[4tln]], [[5tln]], [[1pe5]], [[3ms3]], [[3msa]], [[3msf]], [[3msn]], [[3n21]], [[3nn7]], [[3t73]], [[3t74]], [[3t87]], [[3t8c]], [[3t8d]], [[3t8f]], [[3t8g]], [[3t8h]], [[4h57]], [[4d9w]], [[4d91]] – TML+inhibitor<br /> | **[[3for]], [[1y3g]], [[1zdp]], [[1z9g]], [[1pes]], [[1pe7]], [[1pe8]], [[1os0]], [[1kto]], [[1ks7]], [[1kro]], [[1kr6]], [[1kkk]], [[1kjo]], [[1kjp]], [[1qf0]], [[1qf1]], [[1qf2]], [[1hyt]], [[1thl]], [[6tmn]], [[7tln]], [[4tln]], [[5tln]], [[1pe5]], [[3ms3]], [[3msa]], [[3msf]], [[3msn]], [[3n21]], [[3nn7]], [[3t73]], [[3t74]], [[3t87]], [[3t8c]], [[3t8d]], [[3t8f]], [[3t8g]], [[3t8h]], [[4h57]], [[4d9w]], [[4d91]], [[5dpe]], [[5dpf]], [[5js3]], [[5jss]], [[5jt9]], [[5jvi]], [[5jxn]], [[5lif]], [[5lvd]], [[5lwd]], [[5m5f]], [[5m69]], [[5mnr]], [[5n2t]], [[5n2x]], [[5n2z]], [[5n31]], [[5n34]], [[5n3v]], [[5n3y]], [[5ma7]], [[5l3u]], [[5l41]], [[5l8p]], [[5m9w]], [[6tmn]], [[7tln]], [[5tln]], [[5tmn]] – TML+inhibitor<br /> | ||
**[[3ssb]] – TML + Impi-α<br /> | **[[3ssb]] – TML + Impi-α<br /> | ||
**[[3t2h]] – TML + trimethylamine oxide<br /> | **[[3t2h]] – TML + trimethylamine oxide<br /> | ||
Revision as of 01:34, 7 October 2017
FunctionThermolysin (TML) is a thermostable metalloproteinase enzyme from Bacillus thermoproteolyticus. It catalyzes the hydrolysis of peptide bonds containing hydrophobic residues. See Metalloproteases and Matrix metalloproteinase for discussion. Structural highlightsThermolysin is a well researched metalloprotease containing (click this!) and the amino acids His-Glu-X-His-His as its catalytic center. , holding it fast, while stabilize the substrate protein which will be cleaved into two smaller proteins.[1][2]. |
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3D Structures of Thermolysin3D Structures of Thermolysin
Updated on 07-October-2017
ReferencesReferences
- ↑ Matthews, BW. (1988): Structural basis of the action of thermolysin and related zinc peptidases. In: Acc. Chem. Res. 21(9); 333–340; http://dx.doi.org/10.1021/ar00153a003
- ↑ Pelmenschikov V, Blomberg MR, Siegbahn PE. A theoretical study of the mechanism for peptide hydrolysis by thermolysin. J Biol Inorg Chem. 2002 Mar;7(3):284-98. Epub 2001 Sep 27. PMID:11935352 doi:http://dx.doi.org/10.1007/s007750100295