Bacterial leucyl aminopeptidase

Details

Name
Bacterial leucyl aminopeptidase
Kind
protein
Synonyms
  • 3.4.11.10
Gene Name
Not Available
UniProtKB Entry
Q01693Swiss-Prot
Organism
Vibrio proteolyticus
NCBI Taxonomy ID
671
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
Not Available
Specific Function
aminopeptidase activity
Pfam Domain Function
Signal Regions
1-21
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
PDB ID(s)1AMP, 1CP6, 1FT7, 1IGB, 1LOK, 1RTQ, 1TXR, 1XRY, 2ANP, 2DEA, 2IQ6, 2NYQ, 2PRQ, 3B35, 3B3C, 3B3S, 3B3T, 3B3V, 3B3W, 3B7I, 3FH4, 3VH9
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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Para-Iodo-D-Phenylalanine Hydroxamic AcidexperimentalunknowntargetDetails
Leucine Phosphonic AcidexperimentalunknowntargetDetails
1-Butane Boronic AcidexperimentalunknowntargetDetails
UbenimexinvestigationalunknowntargetDetails