Bacterial leucyl aminopeptidase
Details
- Name
- Bacterial leucyl aminopeptidase
- Synonyms
- 3.4.11.10
- Gene Name
- Not Available
- Organism
- Vibrio proteolyticus
- Amino acid sequence
>lcl|BSEQ0016411|Bacterial leucyl aminopeptidase MKYTKTLLAMVLSATFCQAYAEDKVWISIGADANQTVMKSGAESILPNSVASSGQVWVGQ VDVAQLAELSHNMHEEHNRCGGYMVHPSAQSAMAASAMPTTLASFVMPPITQQATVTAWL PQVDASQITGTISSLESFTNRFYTTTSGAQASDWIASEWQALSASLPNASVKQVSHSGYN QKSVVMTITGSEAPDEWIVIGGHLDSTIGSHTNEQSVAPGADDDASGIAAVTEVIRVLSE NNFQPKRSIAFMAYAAEEVGLRGSQDLANQYKSEGKNVVSALQLDMTNYKGSAQDVVFIT DYTDSNFTQYLTQLMDEYLPSLTYGFDTCGYACSDHASWHNAGYPAAMPFESKFNDYNPR IHTTQDTLANSDPTGSHAKKFTQLGLAYAIEMGSATGDTPTPGNQLEDGVPVTDLSGSRG SNVWYTFELETQKNLQITTSGGYGDLDLYVKFGSKASKQNWDCRPYLSGNNEVCTFNNAS PGTYSVMLTGYSNYSGASLKASTF
- Number of residues
- 504
- Molecular Weight
- 54231.585
- Theoretical pI
- 4.49
- GO Classification
- Functionsaminopeptidase activity / metal ion bindingComponentsextracellular region
- General Function
- Metal ion binding
- Specific Function
- Not Available
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0002768|1515 bp ATGAAATATACCAAAACGTTACTGGCTATGGTTCTTTCCGCCACTTTTTGTCAGGCTTAC GCCGAAGACAAAGTGTGGATCTCAATTGGTGCGGACGCCAATCAAACGGTGATGAAGTCC GGGGCAGAATCCATTCTTCCGAATTCCGTCGCCAGCAGTGGTCAGGTGTGGGTTGGACAA GTCGATGTCGCTCAGCTCGCTGAGCTTTCGCATAATATGCACGAAGAGCATAATCGCTGT GGTGGGTACATGGTACACCCTTCAGCGCAAAGTGCGATGGCGGCAAGTGCGATGCCCACT ACGCTAGCCAGCTTCGTGATGCCGCCGATTACACAGCAGGCGACCGTCACAGCGTGGCTG CCTCAGGTTGACGCGTCACAAATCACCGGGACCATCAGTTCGCTGGAGAGCTTCACCAAC CGTTTTTACACCACCACTTCTGGAGCTCAGGCCTCGGACTGGATAGCCAGCGAATGGCAG GCTCTGTCAGCCTCTCTGCCCAATGCCAGCGTCAAGCAAGTGTCTCACTCAGGCTACAAC CAAAAGTCGGTCGTTATGACCATTACAGGCTCAGAAGCGCCTGACGAGTGGATTGTGATT GGTGGTCACCTTGATTCGACCATTGGTTCACACACCAACGAACAAAGTGTTGCACCGGGT GCGGATGATGATGCTTCGGGTATCGCAGCCGTCACTGAAGTGATCCGTGTGCTGTCAGAG AACAACTTCCAACCAAAACGTAGCATTGCCTTCATGGCTTATGCCGCTGAGGAAGTCGGC TTGCGTGGTTCACAAGATCTGGCGAATCAGTATAAATCCGAAGGTAAAAACGTGGTTTCC GCCCTGCAACTGGACATGACCAACTACAAAGGTTCTGCCCAAGATGTCGTGTTTATCACC GATTACACTGACAGCAACTTCACTCAATATCTGACGCAGCTAATGGACGAGTATTTGCCG AGTCTGACTTACGGTTTCGATACTTGCGGGTACGCCTGTTCTGATCACGCATCATGGCAC AACGCTGGCTACCCCGCCGCCATGCCGTTTGAGTCGAAGTTCAACGATTACAATCCGCGT ATTCACACCACTCAAGATACGTTGGCGAACTCCGATCCAACCGGCTCTCATGCCAAGAAG TTCACTCAGTTAGGTCTTGCTTATGCGATTGAAATGGGCAGCGCAACCGGTGACACACCA ACACCAGGCAATCAGCTGGAAGACGGTGTGCCTGTCACCGATTTGTCTGGTAGCCGAGGC AGCAACGTATGGTATACGTTTGAACTGGAAACCCAGAAAAACCTGCAAATCACCACCTCT GGTGGCTATGGTGATCTGGACTTGTATGTGAAGTTTGGCAGTAAAGCCAGCAAACAGAAC TGGGATTGCCGCCCATATCTCAGTGGGAACAACGAAGTCTGTACGTTCAACAATGCTTCA CCAGGCACCTACTCCGTCATGCTGACAGGGTACTCCAACTACAGCGGAGCCAGCCTGAAA GCCAGCACTTTCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q01693 UniProtKB Entry Name AMPX_VIBPR GenBank Protein ID 48474 GenBank Gene ID Z11993 - General References
- Van Heeke G, Denslow S, Watkins JR, Wilson KJ, Wagner FW: Cloning and nucleotide sequence of the Vibrio proteolyticus aminopeptidase gene. Biochim Biophys Acta. 1992 Jul 15;1131(3):337-40. [Article]
- Guenet C, Lepage P, Harris BA: Isolation of the leucine aminopeptidase gene from Aeromonas proteolytica. Evidence for an enzyme precursor. J Biol Chem. 1992 Apr 25;267(12):8390-5. [Article]
- Schalk C, Remy JM, Chevrier B, Moras D, Tarnus C: Rapid purification of the Aeromonas proteolytica aminopeptidase: crystallization and preliminary X-ray data. Arch Biochem Biophys. 1992 Apr;294(1):91-7. [Article]
- Chevrier B, Schalk C, D'Orchymont H, Rondeau JM, Moras D, Tarnus C: Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family. Structure. 1994 Apr 15;2(4):283-91. [Article]
- Chevrier B, D'Orchymont H, Schalk C, Tarnus C, Moras D: The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit. Eur J Biochem. 1996 Apr 15;237(2):393-8. [Article]
- De Paola CC, Bennett B, Holz RC, Ringe D, Petsko GA: 1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development. Biochemistry. 1999 Jul 13;38(28):9048-53. [Article]
- Stamper C, Bennett B, Edwards T, Holz RC, Ringe D, Petsko G: Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis. Biochemistry. 2001 Jun 19;40(24):7035-46. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01980 Para-Iodo-D-Phenylalanine Hydroxamic Acid experimental unknown Details DB02386 Leucine Phosphonic Acid experimental unknown Details DB02664 1-Butane Boronic Acid experimental unknown Details DB03424 Ubenimex investigational unknown Details