Methionine aminopeptidase

Details

Name
Methionine aminopeptidase
Synonyms
  • 3.4.11.18
  • MAP
  • Peptidase M
Gene Name
map
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011450|Methionine aminopeptidase
MAISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQHAVSACL
GYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIKDGFHGDTSKMFIVGKPTI
MGERLCRITQESLYLALRMVKPGINLREIGAAIQKFVEAEGFSVVREYCGHGIGRGFHEE
PQVLHYDSRETNVVLKPGMTFTIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVV
TDNGCEILTLRKDDTIPAIISHDE
Number of residues
264
Molecular Weight
29330.585
Theoretical pI
5.83
GO Classification
Functions
ferrous iron binding / metalloaminopeptidase activity
Processes
protein initiator methionine removal
Components
cytosol
General Function
Metalloaminopeptidase activity
Specific Function
Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0011451|Methionine aminopeptidase (map)
ATGGCTATCTCAATCAAGACCCCAGAAGATATCGAAAAAATGCGCGTCGCTGGCCGACTG
GCTGCCGAAGTGCTGGAGATGATCGAACCGTATGTTAAACCGGGCGTCAGCACCGGCGAG
CTGGATCGCATCTGTAATGATTACATTGTTAATGAACAACACGCGGTTTCTGCCTGCCTC
GGCTATCACGGCTATCCGAAATCCGTTTGCATCTCTATTAATGAAGTGGTGTGCCACGGT
ATCCCGGACGATGCTAAGCTGCTGAAAGATGGCGATATCGTTAACATTGATGTCACCGTA
ATCAAAGATGGTTTCCACGGCGATACCTCGAAAATGTTTATCGTCGGTAAGCCGACCATC
ATGGGCGAACGTCTGTGCCGCATCACGCAAGAAAGCCTGTACCTGGCGCTACGCATGGTA
AAACCAGGCATTAATCTGCGCGAAATCGGTGCGGCGATTCAGAAATTTGTCGAAGCAGAA
GGCTTCTCCGTCGTTCGTGAATATTGCGGACACGGTATTGGTCGCGGCTTCCATGAAGAA
CCGCAGGTGCTGCACTATGACTCCCGTGAAACCAACGTCGTACTGAAACCTGGGATGACG
TTCACCATCGAGCCAATGGTCAACGCGGGTAAAAAAGAGATCCGCACCATGAAAGATGGC
TGGACGGTAAAAACCAAAGATCGCAGCTTGTCTGCACAATATGAGCATACTATTGTGGTG
ACTGATAACGGCTGCGAAATTCTGACGCTACGCAAGGATGACACCATCCCGGCGATAATC
TCGCACGACGAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AE18
UniProtKB Entry NameMAP1_ECOLI
GenBank Protein ID146727
GenBank Gene IDM15106
General References
  1. Ben-Bassat A, Bauer K, Chang SY, Myambo K, Boosman A, Chang S: Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure. J Bacteriol. 1987 Feb;169(2):751-7. [Article]
  2. Fujita N, Mori H, Yura T, Ishihama A: Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region. Nucleic Acids Res. 1994 May 11;22(9):1637-9. [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. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  6. D'souza VM, Holz RC: The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme. Biochemistry. 1999 Aug 24;38(34):11079-85. [Article]
  7. D'souza VM, Bennett B, Copik AJ, Holz RC: Divalent metal binding properties of the methionyl aminopeptidase from Escherichia coli. Biochemistry. 2000 Apr 4;39(13):3817-26. [Article]
  8. Copik AJ, Swierczek SI, Lowther WT, D'souza VM, Matthews BW, Holz RC: Kinetic and spectroscopic characterization of the H178A methionyl aminopeptidase from Escherichia coli. Biochemistry. 2003 May 27;42(20):6283-92. [Article]
  9. Watterson SJ, Mitra S, Swierczek SI, Bennett B, Holz RC: Kinetic and spectroscopic analysis of the catalytic role of H79 in the methionine aminopeptidase from Escherichia coli. Biochemistry. 2008 Nov 11;47(45):11885-93. doi: 10.1021/bi801499g. Epub 2008 Oct 15. [Article]
  10. Mitra S, Job KM, Meng L, Bennett B, Holz RC: Analyzing the catalytic role of Asp97 in the methionine aminopeptidase from Escherichia coli. FEBS J. 2008 Dec;275(24):6248-59. doi: 10.1111/j.1742-4658.2008.06749.x. Epub 2008 Nov 13. [Article]
  11. Chai SC, Ye QZ: Analysis of the stoichiometric metal activation of methionine aminopeptidase. BMC Biochem. 2009 Dec 17;10:32. doi: 10.1186/1471-2091-10-32. [Article]
  12. Xiao Q, Zhang F, Nacev BA, Liu JO, Pei D: Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases. Biochemistry. 2010 Jul 6;49(26):5588-99. doi: 10.1021/bi1005464. [Article]
  13. Sule N, Singh RK, Zhao P, Srivastava DK: Probing the metal ion selectivity in methionine aminopeptidase via changes in the luminescence properties of the enzyme bound europium ion. J Inorg Biochem. 2012 Jan;106(1):84-9. doi: 10.1016/j.jinorgbio.2011.09.020. Epub 2011 Sep 22. [Article]
  14. Roderick SL, Matthews BW: Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme. Biochemistry. 1993 Apr 20;32(15):3907-12. [Article]
  15. Lowther WT, Orville AM, Madden DT, Lim S, Rich DH, Matthews BW: Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis. Biochemistry. 1999 Jun 15;38(24):7678-88. [Article]
  16. Lowther WT, Zhang Y, Sampson PB, Honek JF, Matthews BW: Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues. Biochemistry. 1999 Nov 9;38(45):14810-9. [Article]
  17. Ye QZ, Xie SX, Ma ZQ, Huang M, Hanzlik RP: Structural basis of catalysis by monometalated methionine aminopeptidase. Proc Natl Acad Sci U S A. 2006 Jun 20;103(25):9470-5. Epub 2006 Jun 12. [Article]
  18. Ma ZQ, Xie SX, Huang QQ, Nan FJ, Hurley TD, Ye QZ: Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymes. BMC Struct Biol. 2007 Dec 19;7:84. [Article]
  19. Evdokimov AG, Pokross M, Walter RL, Mekel M, Barnett BL, Amburgey J, Seibel WL, Soper SJ, Djung JF, Fairweather N, Diven C, Rastogi V, Grinius L, Klanke C, Siehnel R, Twinem T, Andrews R, Curnow A: Serendipitous discovery of novel bacterial methionine aminopeptidase inhibitors. Proteins. 2007 Feb 15;66(3):538-46. [Article]
  20. Wang WL, Chai SC, Huang M, He HZ, Hurley TD, Ye QZ: Discovery of inhibitors of Escherichia coli methionine aminopeptidase with the Fe(II)-form selectivity and antibacterial activity. J Med Chem. 2008 Oct 9;51(19):6110-20. doi: 10.1021/jm8005788. Epub 2008 Sep 12. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02088Norleucine PhosphonateexperimentalunknownDetails
DB02151Methionine PhosphonateexperimentalunknownDetails
DB029095-(2-Chlorophenyl)Furan-2-Carboxylic AcidexperimentalunknownDetails
DB03799TrifluoromethionineexperimentalunknownDetails
DB04015Methionine PhosphinateexperimentalunknownDetails
DB073045-[2-(TRIFLUOROMETHOXY)PHENYL]-2-FUROIC ACIDexperimentalunknownDetails
DB073055-(2-CHLORO-4-NITROPHENYL)-2-FUROIC ACIDexperimentalunknownDetails
DB073085-(2-CHLOROBENZYL)-2-FUROIC ACIDexperimentalunknownDetails
DB074075-(2-METHOXYPHENYL)-2-FUROIC ACIDexperimentalunknownDetails
DB074085-(2-NITROPHENYL)-2-FUROIC ACIDexperimentalunknownDetails
DB07591N1-CYCLOPENTYL-N2-(THIAZOL-2-YL)OXALAMIDEexperimentalunknownDetails
DB077585-(2,5-DICHLOROPHENYL)-2-FUROIC ACIDexperimentalunknownDetails
DB077595-[2-(TRIFLUOROMETHYL)PHENYL]-2-FUROIC ACIDexperimentalunknownDetails
DB08451N-(QUINOLIN-8-YL)METHANESULFONAMIDEexperimentalunknownDetails
DB086665-imino-4-(3-trifluoromethyl-phenylazo)-5H-pyrazol-3-ylamineexperimentalunknownDetails
DB086674-(4-fluoro-phenylazo)-5-imino-5H-pyrazol-3-ylamineexperimentalunknownDetails
DB086683-(5-Amino-3-imino-3H-pyrazol-4-ylazo)-benzoic acidexperimentalunknownDetails
DB08669METHYL N-[(2S,3R)-3-AMINO-2-HYDROXY-3-(4-METHYLPHENYL)PROPANOYL]-D-ALANYL-D-LEUCINATEexperimentalunknownDetails
DB08670METHYL N-[(2S,3R)-3-AMINO-2-HYDROXY-3-(4-ISOPROPYLPHENYL)PROPANOYL]-D-ALANYL-D-LEUCINATEexperimentalunknownDetails
DB086715-Imino-4-(2-trifluoromethyl-phenylazo)-5H-pyrazol-3-ylamineexperimentalunknownDetails
DB087184-(3-ethylthiophen-2-yl)benzene-1,2-diolexperimentalunknownDetails
DB087575-(2-chlorophenyl)furan-2-carbohydrazideexperimentalunknownDetails
DB08758IMIDAZO[2,1-A]ISOQUINOLINE-2-CARBOHYDRAZIDEexperimentalunknownDetails