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
Functions
metal ion binding / metalloendopeptidase activity
Components
extracellular 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
ResourceLink
UniProtKB IDP00800
UniProtKB Entry NameTHER_BACTH
GenBank Protein ID441267
GenBank Gene IDX76986
General References
  1. 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. [PubMed:8002967]
  2. 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. [PubMed:5040648]
  3. Burstein Y, Walsh KA, Neurath H: Evidence of an essential histidine residue in thermolysin. Biochemistry. 1974 Jan 1;13(1):205-10. [PubMed:4808703]
  4. Holmes MA, Matthews BW: Structure of thermolysin refined at 1.6 A resolution. J Mol Biol. 1982 Oct 5;160(4):623-39. [PubMed:7175940]
  5. Matthews BW, Weaver LH, Kester WR: The conformation of thermolysin. J Biol Chem. 1974 Dec 25;249(24):8030-44. [PubMed:4214815]
  6. 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. [PubMed:7993910]
  7. 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. [PubMed:9305992]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB071032-(4-METHYLPHENOXY)ETHYLPHOSPHINATEexperimentalunknownDetails
DB07434HONH-BENZYLMALONYL-L-ALANYLGLYCINE-P-NITROANILIDEexperimentalunknownDetails
DB07487(6-METHYL-3,4-DIHYDRO-2H-CHROMEN-2-YL)METHYLPHOSPHINATEexperimentalunknownDetails
DB07506L-BENZYLSUCCINIC ACIDexperimentalunknownDetails
DB06819Phenylbutyric acidapproved, investigationalunknownDetails
DB07673DEAMINO-METHYL-PHENYLALANINEexperimentalunknownDetails
DB079892-(ACETYL-HYDROXY-AMINO)-4-METHYL-PENTANOIC ACID METHYL ESTERexperimentalunknownDetails
DB019353-{[(1r)-1-Benzyl-2-Sulfanylethyl]Amino}-3-Oxopropanoic AcidexperimentalunknownDetails
DB02597[2(R,S)-2-Sulfanylheptanoyl]-Phe-AlaexperimentalunknownDetails
DB02669RB106experimentalunknownDetails