Isoaspartyl dipeptidase

Details

Name
Isoaspartyl dipeptidase
Synonyms
  • 3.4.19.-
  • yjiF
Gene Name
iadA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0016562|Isoaspartyl dipeptidase
MIDYTAAGFTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPNCTVVDLSGQIL
CPGFIDQHVHLIGGGGEAGPTTRTPEVALSRLTEAGVTSVVGLLGTDSISRHPESLLAKT
RALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGVKCAISDHRSAAPDVYHLAN
MAAESRVGGLLGGKPGVTVFHMGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQ
ALEFARKGGTIDITSSIDEPVAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLT
HIGVAGFETLLETVQVLVKDYDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMT
PELRIEQVYARGKLMVKDGKACVKGTFETA
Number of residues
390
Molecular Weight
41083.515
Theoretical pI
4.89
GO Classification
Functions
beta-aspartyl-peptidase activity / hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds / metallopeptidase activity / zinc ion binding
Components
cytoplasm / cytosol
General Function
Zinc ion binding
Specific Function
Catalyzes the hydrolytic cleavage of a subset of L-isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. The best substrate for the enzyme reported thus far is iso-Asp-Leu.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0016563|Isoaspartyl dipeptidase (iadA)
ATGATTGATTATACCGCAGCCGGTTTTACCCTGCTGCAGGGAGCGCATTTGTATGCGCCG
GAAGATCGGGGAATTTGCGATGTCCTCGTCGCTAACGGCAAAATTATCGCCGTTGCCAGC
AATATCCCTTCTGACATTGTACCGAACTGCACGGTTGTCGATCTCAGTGGGCAGATCCTC
TGCCCAGGTTTTATTGATCAACACGTCCATTTGATTGGCGGTGGCGGCGAAGCAGGTCCC
ACGACGCGCACGCCGGAAGTGGCGCTAAGTCGCCTGACGGAAGCGGGCGTCACGTCAGTG
GTTGGTCTGCTGGGCACCGACTCTATCTCTCGCCACCCGGAATCCCTGCTCGCCAAGACC
CGTGCGCTCAATGAAGAAGGCATCAGCGCCTGGATGCTGACCGGCGCTTATCATGTCCCT
TCCCGCACCATTACGGGTTCCGTGGAAAAAGACGTGGCGATTATCGATCGTGTGATTGGC
GTGAAATGCGCCATCTCTGATCACCGTTCTGCCGCACCGGACGTTTATCACCTGGCCAAT
ATGGCGGCAGAATCCCGCGTTGGCGGTTTGCTCGGCGGTAAACCTGGCGTCACCGTGTTC
CACATGGGCGACAGTAAAAAGGCGTTACAGCCTATTTATGACCTGCTGGAAAACTGCGAT
GTGCCGATCAGCAAGCTGCTGCCGACCCACGTTAACCGCAACGTACCGTTGTTTGAGCAG
GCGCTGGAGTTCGCGCGCAAAGGCGGCACCATCGATATCACCAGCAGCATTGACGAACCG
GTCGCCCCTGCCGAAGGTATTGCCCGCGCCGTTCAGGCGGGTATTCCGCTGGCACGCGTC
ACCCTCAGCTCCGACGGCAACGGTAGCCAGCCGTTCTTCGATGACGAAGGGAATTTAACC
CATATCGGTGTTGCCGGTTTTGAAACGTTGCTGGAAACCGTGCAGGTGCTGGTCAAAGAC
TATGATTTCAGTATCAGCGATGCCCTGCGCCCGCTCACCAGTAGCGTAGCCGGTTTCCTT
AACCTGACCGGGAAAGGCGAAATTCTGCCAGGCAATGATGCTGACTTGCTGGTCATGACG
CCAGAACTGCGCATTGAGCAGGTATACGCTCGCGGCAAACTGATGGTCAAAGACGGCAAA
GCCTGCGTGAAAGGAACGTTTGAAACGGCTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP39377
UniProtKB Entry NameIADA_ECOLI
GenBank Protein ID640031
GenBank Gene IDU15029
General References
  1. Gary JD, Clarke S: Purification and characterization of an isoaspartyl dipeptidase from Escherichia coli. J Biol Chem. 1995 Feb 24;270(8):4076-87. [Article]
  2. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Haley EE: Purification and properties of a beta-aspartyl peptidase from Escherichia coli. J Biol Chem. 1968 Nov 10;243(21):5748-52. [Article]
  6. Thoden JB, Marti-Arbona R, Raushel FM, Holden HM: High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli. Biochemistry. 2003 May 6;42(17):4874-82. [Article]
  7. Jozic D, Kaiser JT, Huber R, Bode W, Maskos K: X-ray structure of isoaspartyl dipeptidase from E.coli: a dinuclear zinc peptidase evolved from amidohydrolases. J Mol Biol. 2003 Sep 5;332(1):243-56. [Article]
  8. Marti-Arbona R, Fresquet V, Thoden JB, Davis ML, Holden HM, Raushel FM: Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli. Biochemistry. 2005 May 17;44(19):7115-24. [Article]
  9. Marti-Arbona R, Thoden JB, Holden HM, Raushel FM: Functional significance of Glu-77 and Tyr-137 within the active site of isoaspartyl dipeptidase. Bioorg Chem. 2005 Dec;33(6):448-58. Epub 2005 Nov 11. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02437(5r)-5-Amino-6-Hydroxyhexylcarbamic AcidexperimentalunknownDetails
DB03801Lysine Nz-Carboxylic AcidexperimentalunknownDetails