Thermolysin
Details
- Name
- Thermolysin
- Synonyms
- 3.4.24.27
- Thermostable neutral proteinase
- Gene Name
- npr
- Organism
- Bacillus thermoproteolyticus
- Amino acid sequence
>lcl|BSEQ0012641|Thermolysin MKMKMKLASFGLAAGLAAQVFLPYNALASTEHVTWNQQFQTPQFISGDLLKVNGTSPEEL VYQYVEKNENKFKFHENAKDTLQLKEKKNDNLGFTFMRFQQTYKGIPVFGAVVTSHVKDG TLTALSGTLIPNLDTKGSLKSGKKLSEKQARDIAEKDLVANVTKEVPEYEQGKDTEFVVY VNGDEASLAYVVNLNFLTPEPGNWLYIIDAVDGKILNKFNQLDAAKPGDVKSITGTSTVG VGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTLPGSLWADADNQFFASYDA PAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQMVYGDGDGQ TFIPLSGGIDVVAHELTHAVTDYTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEI GEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGG THYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVASVKQ AFDAVGVK
- Number of residues
- 548
- Molecular Weight
- 60103.515
- Theoretical pI
- 5.63
- GO Classification
- Functionsmetal ion binding / metalloendopeptidase activityComponentsextracellular region
- General Function
- Metalloendopeptidase activity
- Specific Function
- Extracellular zinc metalloprotease.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0007256|1647 bp ATGAAAATGAAAATGAAATTAGCATCGTTTGGTCTTGCAGCAGGACTAGCGGCCCAAGTA TTTTTACCTTACAATGCGCTGGCTTCAACGGAACACGTTACATGGAACCAACAATTTCAA ACCCCTCAATTCATCTCCGGTGATCTGCTGAAAGTGAATGGCACATCCCCAGAAGAACTC GTCTATCAATATGTTGAAAAAAACGAAAACAAGTTTAAATTTCATGAAAACGCTAAGGAT ACTCTACAATTGAAAGAAAAGAAAAATGATAACCTTGGTTTTACGTTTATGCGCTTCCAA CAAACGTATAAAGGGATTCCTGTGTTTGGAGCAGTAGTAACGTCGCACGTGAAAGATGGC ACGCTGACGGCGCTATCAGGGACACTGATTCCGAATTTGGACACGAAAGGATCCTTAAAA AGCGGGAAGAAATTGAGTGAGAAACAAGCGCGTGACATTGCTGAAAAAGATTTAGTGGCA AATGTAACAAAGGAAGTACCGGAATATGAACAGGGAAAAGACACCGAGTTTGTTGTTTAT GTCAATGGGGACGAGGCTTCTTTAGCGTACGTTGTCAATTTAAACTTTTTAACTCCTGAA CCAGGAAACTGGCTGTATATCATTGATGCCGTAGACGGAAAAATTTTAAATAAATTTAAC CAACTTGACGCCGCAAAACCAGGTGATGTGAAGTCGATAACAGGAACATCAACTGTCGGA GTGGGAAGAGGAGTACTTGGTGATCAAAAAAATATTAATACAACCTACTCTACGTACTAC TATTTACAAGATAATACGCGTGGAAATGGGATTTTCACGTATGATGCGAAATACCGTACG ACATTGCCGGGAAGCTTATGGGCAGATGCAGATAACCAATTTTTTGCGAGCTATGATGCT CCAGCGGTTGATGCTCATTATTACGCTGGTGTGACATATGACTACTATAAAAATGTTCAT AACCGTCTCAGTTACGACGGAAATAATGCAGCTATTAGATCATCCGTTCATTATAGCCAA GGCTATAATAACGCATTTTGGAACGGTTCGCAAATGGTGTATGGCGATGGTGATGGTCAA ACATTTATTCCACTTTCTGGTGGTATTGATGTGGTCGCACATGAGTTAACGCATGCGGTA ACCGATTATACAGCCGGACTCATTTATCAAAACGAATCTGGTGCAATTAATGAGGCAATG TCTGATATTTTTGGAACGTTAGTCAAATTTTACGCTAACAAAAATCCAGATTGGGAAATT GGAGAGGATGTGTATACACCTGGTATTTCAGGGGATTCGCTCCGTTCGATGTCCGATCCG GCAAAGTATGGTGATCCAGATCACTATTCAAAGCGCTATACAGGCACGCAAGATAATGGC GGGGTTCATATCAATAGCGGAATTATCAACAAAGCCGCTTATTTGATTAGCCAAGGCGGT ACGCATTACGGTGTGAGTGTTGTCGGAATCGGACGCGATAAATTGGGGAAAATTTTCTAT CGTGCATTAACGCAATATTTAACACCAACGTCCAACTTTAGCCAACTTCGTGCTGCCGCT GTTCAATCAGCCACTGACTTGTACGGTTCGACAAGCCAGGAAGTCGCTTCTGTGAAGCAG GCCTTTGATGCGGTAGGGGTGAAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P00800 UniProtKB Entry Name THER_BACTH GenBank Protein ID 441267 GenBank Gene ID X76986 - General References
- O'Donohue MJ, Roques BP, Beaumont A: Cloning and expression in Bacillus subtilis of the npr gene from Bacillus thermoproteolyticus Rokko coding for the thermostable metalloprotease thermolysin. Biochem J. 1994 Jun 1;300 ( Pt 2):599-603. [Article]
- Titani K, Hermodson MA, Ericsson LH, Walsh KA, Neurath H: Amino acid sequence of thermolysin. Isolation and characterization of the fragments obtained by cleavage with cyanogen bromide. Biochemistry. 1972 Jun 20;11(13):2427-35. [Article]
- Burstein Y, Walsh KA, Neurath H: Evidence of an essential histidine residue in thermolysin. Biochemistry. 1974 Jan 1;13(1):205-10. [Article]
- Holmes MA, Matthews BW: Structure of thermolysin refined at 1.6 A resolution. J Mol Biol. 1982 Oct 5;160(4):623-39. [Article]
- Matthews BW, Weaver LH, Kester WR: The conformation of thermolysin. J Biol Chem. 1974 Dec 25;249(24):8030-44. [Article]
- Rico M, Jimenez MA, Gonzalez C, De Filippis V, Fontana A: NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure. Biochemistry. 1994 Dec 13;33(49):14834-47. [Article]
- Conejero-Lara F, Gonzalez C, Jimenez MA, Padmanabhan S, Mateo PL, Rico M: NMR solution structure of the 205-316 C-terminal fragment of thermolysin. An example of dimerization coupled to partial unfolding. Biochemistry. 1997 Sep 30;36(39):11975-83. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB03255 Phenol approved, experimental unknown Details DB07103 2-(4-METHYLPHENOXY)ETHYLPHOSPHINATE experimental unknown Details DB07434 HONH-BENZYLMALONYL-L-ALANYLGLYCINE-P-NITROANILIDE experimental unknown Details DB07487 (6-METHYL-3,4-DIHYDRO-2H-CHROMEN-2-YL)METHYLPHOSPHINATE experimental unknown Details DB07506 L-BENZYLSUCCINIC ACID experimental unknown Details DB07673 (2S)-2-Methyl-3-phenylpropanoic acid experimental unknown Details DB07989 2-(ACETYL-HYDROXY-AMINO)-4-METHYL-PENTANOIC ACID METHYL ESTER experimental unknown Details DB01935 3-{[(1r)-1-Benzyl-2-Sulfanylethyl]Amino}-3-Oxopropanoic Acid experimental unknown Details DB02597 [2(R,S)-2-Sulfanylheptanoyl]-Phe-Ala experimental unknown Details DB02669 RB106 experimental unknown Details