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
Functions
aminopeptidase activity / metal ion binding
Components
extracellular 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
ResourceLink
UniProtKB IDQ01693
UniProtKB Entry NameAMPX_VIBPR
GenBank Protein ID48474
GenBank Gene IDZ11993
General References
  1. 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. [PubMed:1627651]
  2. 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. [PubMed:1569090]
  3. 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. [PubMed:1550363]
  4. 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. [PubMed:8087555]
  5. 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. [PubMed:8647077]
  6. 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. [PubMed:10413478]
  7. 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. [PubMed:11401547]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01980Para-Iodo-D-Phenylalanine Hydroxamic AcidexperimentalunknownDetails
DB02386Leucine Phosphonic AcidexperimentalunknownDetails
DB026641-Butane Boronic AcidexperimentalunknownDetails
DB03424Ubenimexexperimental, investigationalunknownDetails