Literature for peptidase M01.005: alanyl aminopeptidase (bacterial-type)

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Pharma

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    2015
  1. Ganji,R.J., Reddi,R., Gumpena,R., Marapaka,A.K., Arya,T., Sankoju,P., Bhukya,S. and Addlagatta,A.
    Structural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: crystal structure in complex with E. coli aminopeptidase N
    Protein Sci24, 823-831. PubMed  Europe PubMed DOI  S  I
  2. 2012
  3. Gumpena,R., Kishor,C., Ganji,R.J., Jain,N. and Addlagatta,A.
    Glu121-Lys319 salt bridge between catalytic and N-terminal domains is pivotal for the activity and stability of Escherichia coli aminopeptidase N
    Protein Sci21, 727-736. PubMed  Europe PubMed DOI  S
  4. 2009
  5. Fournie-Zaluski,M.C., Poras,H., Roques,B.P., Nakajima,Y., Ito,K. and Yoshimoto,T.
    Structure of aminopeptidase N from Escherichia coli complexed with the transition-state analogue aminophosphinic inhibitor PL250
    Acta Crystallogr D Biol Crystallogr65, 814-822. PubMed  Europe PubMed DOI  S  I
  6. 2008
  7. Addlagatta,A., Gay,L. and Matthews,B.W.
    Structural basis for the unusual specificity of Escherichia coli aminopeptidase N
    Biochemistry47, 5303-5311. PubMed  Europe PubMed DOI  P  S
  8. Nocek,B., Mulligan,R., Bargassa,M., Collart,F. and Joachimiak,A.
    Crystal structure of aminopeptidase N from human pathogen Neisseria meningitidis
    Proteins70, 273-279. PubMed  Europe PubMed DOI  S
  9. 2006
  10. Addlagatta,A., Gay,L. and Matthews,B.W.
    Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site
    Proc Natl Acad Sci U S A103, 13339-13344. PubMed  Europe PubMed DOI  S  I
  11. Ito,K., Nakajima,Y., Onohara,Y., Takeo,M., Nakashima,K., Matsubara,F., Ito,T. and Yoshimoto,T.
    Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition
    J Biol Chem281, 33664-33676. PubMed  Europe PubMed DOI  S