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PMID: 8146141 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 91 ·No. 7 ·1994-03-29 ·Pages 2473-7

Bazan JF, Weaver LH, Roderick SL, Huber R, Matthews BW

Abstract

Amino acid sequence comparison suggests that the structure of Escherichia coli methionine aminopeptidase (EC 3.4.11.18) and the C-terminal domain of Pseudomonas putida creatinase (EC 3.5.3.3) are related. A detailed comparison of the three-dimensional folds of the two enzymes confirms this homology: with an approximately 260-residue chain segment, 218 C alpha atoms of the structures superimpose within 2.5 A; only 41 of these overlapping positions (i.e., 19%) feature identical amino acids in the two protein chains. Notwithstanding this striking correspondence in structure, methionine aminopeptidase binds and is stimulated by Co2+, while creatinase is not a metal-dependent enzyme. Searches of protein data banks using sequence and structure-based profiles reveal other enzymes, including aminopeptidase P (EC 3.4.11.9), prolidase (EC 3.4.13.9), and agropine synthase, that likely share the same "pita-bread" fold common to creatinase and methionine aminopeptidase.

MeSH Terms
Amino Acid Sequence Aminopeptidases/chemistry Dipeptidases/chemistry Escherichia coli/enzymology Methionyl Aminopeptidases Models, Molecular Molecular Sequence Data Protein Conformation Pseudomonas putida/enzymology Sequence Homology, Amino Acid Ureohydrolases/chemistry
Chemicals
Aminopeptidases Methionyl Aminopeptidases X-Pro aminopeptidase Dipeptidases proline dipeptidase Ureohydrolases creatinase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Bazan J F
Institute of Molecular Biology, Howard Hughes Medical Institute, Eugene, OR.
Weaver L H
Roderick S L
Huber R
Matthews B W
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.91.7.2473
Published
1994-03-29
Pages
2473-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC43391
Subset
IM
Grants
NIGMS NIH HHS · GM20066 · United States
External Links
PubMed source DOI: 10.1073/pnas.91.7.2473 PMC Full Text View journal details
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