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
- Functionsferrous iron binding / metalloaminopeptidase activityProcessesprotein initiator methionine removalComponentscytosol
- 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
- Peptidase_M24 (PF00557)
- 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
Resource Link UniProtKB ID P0AE18 UniProtKB Entry Name MAP1_ECOLI GenBank Protein ID 146727 GenBank Gene ID M15106 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details DB02088 Norleucine Phosphonate experimental unknown Details DB02151 Methionine Phosphonate experimental unknown Details DB02909 5-(2-Chlorophenyl)Furan-2-Carboxylic Acid experimental unknown Details DB03799 Trifluoromethionine experimental unknown Details DB04015 Methionine Phosphinate experimental unknown Details DB07304 5-[2-(TRIFLUOROMETHOXY)PHENYL]-2-FUROIC ACID experimental unknown Details DB07305 5-(2-CHLORO-4-NITROPHENYL)-2-FUROIC ACID experimental unknown Details DB07308 5-(2-CHLOROBENZYL)-2-FUROIC ACID experimental unknown Details DB07407 5-(2-METHOXYPHENYL)-2-FUROIC ACID experimental unknown Details DB07408 5-(2-NITROPHENYL)-2-FUROIC ACID experimental unknown Details DB07591 N1-CYCLOPENTYL-N2-(THIAZOL-2-YL)OXALAMIDE experimental unknown Details DB07758 5-(2,5-DICHLOROPHENYL)-2-FUROIC ACID experimental unknown Details DB07759 5-[2-(TRIFLUOROMETHYL)PHENYL]-2-FUROIC ACID experimental unknown Details DB08451 N-(QUINOLIN-8-YL)METHANESULFONAMIDE experimental unknown Details DB08666 5-imino-4-(3-trifluoromethyl-phenylazo)-5H-pyrazol-3-ylamine experimental unknown Details DB08667 4-(4-fluoro-phenylazo)-5-imino-5H-pyrazol-3-ylamine experimental unknown Details DB08668 3-(5-Amino-3-imino-3H-pyrazol-4-ylazo)-benzoic acid experimental unknown Details DB08669 METHYL N-[(2S,3R)-3-AMINO-2-HYDROXY-3-(4-METHYLPHENYL)PROPANOYL]-D-ALANYL-D-LEUCINATE experimental unknown Details DB08670 METHYL N-[(2S,3R)-3-AMINO-2-HYDROXY-3-(4-ISOPROPYLPHENYL)PROPANOYL]-D-ALANYL-D-LEUCINATE experimental unknown Details DB08671 5-Imino-4-(2-trifluoromethyl-phenylazo)-5H-pyrazol-3-ylamine experimental unknown Details DB08718 4-(3-ethylthiophen-2-yl)benzene-1,2-diol experimental unknown Details DB08757 5-(2-chlorophenyl)furan-2-carbohydrazide experimental unknown Details DB08758 IMIDAZO[2,1-A]ISOQUINOLINE-2-CARBOHYDRAZIDE experimental unknown Details