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spinqualitylabelsall models Bacterial leucine aminopeptidase complex with 8-hydroxyquinoline, glycerol, SCN, Zn+2 (magenta), Na+ (cyan) and Cl- (green) ions (PDB code 3vh9) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Aminopeptidase from Aeromonas proteolytica[2] 3 S. griseus aminopeptidase Function Aminopeptidases (AP) (EC 3) are metal - mostly Zn-dependent enzymes involved in the digestion of proteins. Cytosol AP (Cyt-AP), deblocking AP (DAP) and AP N (APN) remove N-terminal amino acids. The AP are classified by the amino acid which they hydrolyze. Other types of AP are: Cold-activated AP (Col-AP) Heat stable AP from Thermus thermophilus (AmpT) AP from Staphylococcus aureus (AmpS) SGAP from Stereomyces griseus. See details in Streptomyces griseus Aminopeptidase (SGAP). Alanine aminopeptidase is called aminopeptidase N. See details in Aminopeptidase N. Aminopeptidases catalyze a release of an N-terminal amino acid from a peptide, amide, or arylamide. Beta-peptidyl AP (BapA) cleaves N-terminal β-homoamino acid from peptides of length 2 to 6.[1] Aminopeptidase from Aeromonas proteolytica[2] The selective inhibition of an , a hydrolase, by derivatives is reported. Based on our findings about 8-HQ-based Zn2+ fluorophores, it was hypothesized that 8-HQ derivatives have the potential to function as specific inhibitors of Zn2+ enzymes, especially dinuclear Zn2+ hydrolases. Inhibitory assays of 8-HQ derivatives against AAP disclosed that the 8-HQ and 5-substituted 8-HQ′s are competitive inhibitors for AAP with inhibition constants (Ki) of 0.16—29 μM at pH 8.0. (1.3 Å resolution) as well as fluorescence titrations of these drugs with AAP confirmed that , in which the in the active site of AAP and the (PDB code: 3vh9). of free AAP (colored green) containing Zn2+-bound water molecule (H2O or OH-; red sphere) (1rtq) bridging two Zn2+ and AAP–8-HQ complex (darkmagenta, 3vh9). Two Zn2+ are depicted as magenta spheres. S. griseus aminopeptidase S. griseus aminopeptidase (SGAP) cleaves the N-terminal amino acid from a peptide or protein, and is specific for larger hydrophobic acids, especially leucine. No cleavage occurs if the next residue is proline. The of the enzyme contains two Zn2+ ions with His85 and Asp160 as ligands for one ion, and Glu132 and His247 as ligands for the second ion. Asp97 is a common ligand to both ions. What appears to be a phosphate anion is bound to both zinc atoms, replacing the water molecule/hydroxide ion normally found in this class of enzyme. See details of SGAP in Streptomyces griseus Aminopeptidase (SGAP).

3D Structures of Aminopeptidase

Updated on 02-March-2017 {{#tree:id=OrganizedByTopic|openlevels=0|

• Cysteine aminopeptidase

• • 3pw3 – PdCys-AP – Parabacteroides distasonis

• Glutamic acid aminopeptidase

• • 2wyr – PhGlu-AP+Co – Pyrococcus horikoshii
    
  • 3kl9 – SpGlu-AP – Streptococcus pneumoniae
    
  • 4kx7 – hGlu-AP + Zn – human
    
  • 4kx8, 4kxb – hGlu-AP + Zn + statin derivative
    
  • 4kx9, 4kxa, 4kxc, 4kxd – hGlu-AP + Zn + amino acid
    

• Alanine aminopeptidase

• • 3ebg – PfAla-AP - Plasmodium falciparum
    
  • 3ebh - PfAla-AP+bestatin
    
  • 3ebi - PfAla-AP+dipeptide analog
    
  • 4r5t, 4r5v, 4r5x – PfAla-AP + inhibitor
    
  • 4fke – pAla-AP + Zn – pig
    
  • 4fkh – pAla-AP + Zn + alanine
    
  • 4naq, 4nz8 – pAla-AP + Zn + polyalanine
    
  • 4hom – pAla-AP + Zn + substance P
    
  • 4fkk – pAla-AP + Zn + bestatin
    
  • 4f5c – pAla-AP + PRCV spike protein + Zn
    
  • 4fyq - hAla-AP + Zn
    
  • 4fyr - hAla-AP + Zn + bestatin
    
  • 4fys - hAla-AP + Zn + angiotensin
    
  • 4fyt - hAla-AP + Zn + amastatin
    

• Aminopeptidase N

• • 3ked – EcAPN+2,4-diaminobutyric acid – Escherichia coli
    
  • 2hpo, 2dq6, 3puu – EcAPN
    
  • 2hpt, 2dqm – EcAPN+bestatin
    
  • 2zxg – EcAPN+transition state analog
    
  • 3b2p, 3b2x, 3b34, 3b37, 3b3b, 3qjx, 4xo5, 4xo4, 4xo3, 4xnd, 4xnb, 4xna, 4xn9, 4xn8, 4xn7, 4xn5, 4xn4, 4xn2, 4xn1, 4xmz, 4xmx, 4xmw, 4xmv, 4xmu, 4xmt – EcAPN + Zn +amino acid
    
  • 4q4i – EcAPN+ Zn + peptide
    
  • 4q4e – EcAPN+ Zn + actinonin
    
  • 4ou3 – pAPN+ Zn + peptide
    
  • 2gtq – NmAPN – Neisseria meningitides
    
  • 5dyf – NmAPN + benzyl-diaminoethylphosphonate
    
  • 4pu2, 4pvb – NmAP N + Leu analog
    
  • 4pw4 – NmAP N + Phe analog
    
  • 4qhp, 4qir, 4qme, 4qpe, 4quo – NmAP N + dipeptide analog
    
  • 5dll – FtAPN - Francisella tularensis
    
  • 4fgm – AP N + Zn – Idiomarina loihiensis
    

• Proline aminopeptidase

• • 3ovk – Xaa Pro-AP – Streptococcus pyogenes
    
  • 3il0 - Xaa Pro-AP – Streptococcus thermophilus
    
  • 2v3x, 2v3y, 2v3z - Xaa EcPro-AP (mutant)+tripeptide
    
  • 5cnx - Xaa EcPro-AP (mutant) + Zn
    
  • 1w7v, 2bh3 - Xaa EcPro-AP+Zn+Mg+polypeptide
    
  • 2bn7 - Xaa EcPro-AP+Zn+Mg+Mn+polypeptide
    
  • 2bha, 2bhd - Xaa EcPro-AP+Mg+polypeptide
    
  • 1a16 - Xaa EcPro-AP+Mn+polypeptide
    
  • 1wbq, 2bhb - Xaa EcPro-AP+Zn+Mg
    
  • 2bhc - Xaa EcPro-AP+Na+Mg
    
  • 1wl6 - Xaa EcPro-AP+Mg
    
  • 1wl9, 1m35, 1jaw - Xaa EcPro-AP+Mn
    
  • 1wlr - Xaa EcPro-AP
    
  • 2bws, 2bwt, 2bwu, 2bwv, 2bww, 2bwx, 2bwy - Xaa EcPro-AP (mutant)
    
  • 1w2m - Xaa EcPro-AP+Ca
    
  • 1n51 – Xaa EcPro-AP+apstatin
    
  • 3ig4 - Xaa Pro-AP+ Mn – Bacillus anthracis
    
  • 4fkc – Xaa TsPro-AP + Cd – Thermococcus sibiricus
    
  • 4rgz – Xaa TsPro-AP + Zn
    
  • 4pv4 – Pro-AP II + Mg – Yersinia pestis
    
  • 2zsg – X TmPro-AP – Thermatoga maritima
    
  • 3ctz – X hPro-AP
    
  • 1x2b, 1x2e, 1wm1 – SmPro-AP + inhibitor – Serratia marcescens
    
  • 1qtr – SmPro-AP
    
  • 1xqv – TaPro-AP (mutant) – Thermoplasma acidophilum
    
  • 1xqw, 1xqx, 1xqy, 1xrl, 1xrm, 1xrn, 1xro, 1xrp, 1xrq, 1xrr – TaPro-AP+polypeptide
    
  • 3azo – SmPro-AP – Streptomyces morookaensis
    
  • 3azp - SmPro-AP (mutant)
    
  • 3azq - SmPro-AP (mutant) + PGG
    

• Leucine aminopeptidase

• • 5jm9, 4r8f – yLeu-AP 1 - yeast
    
  • 5jhc – yLeu-AP 1 (mutant)
    
  • 5jgf – yLeu-AP 1 + Zn
    
  • 5jh9 – yLeu-AP 1 (mutant) + Zn
    
  • 3jru – Leu-AP – Xanthomonas oryzae
    
  • 2hc9, 2hb6 – Leu-AP – Caenorhabditis elegans
    
  • 2ewb – bLeu-AP+zofenoprilat – bovine
    
  • 1lam, 1lap – bLue-AP
    
  • 1bpm, 1bpn – bLue-AP+Zn+Mg
    
  • 2j9a - bLue-AP+Zn + inhibitor
    
  • 1lan, 1lcp – bLue-AP+leucine derivative
    
  • 1bll – bLue-AP+amastatin
    
  • 3qnf – hLeu-AP 1
    
  • 2xdt, 2yd0 – hLeu-AP 1 soluble domain
    
  • 3rjo - hLeu-AP 1 peptide-binding domain
    
  • 3mdj - hLeu-AP 1 soluble domain + inhibitor
    
  • 3h8e, 3h8f, 3h8g – Leu-AP – Pseudomonas putida
    
  • 3kqx, 3kqz, 3kr4, 3kr5 – PfLeu-AP
    
  • 3fh4, 1rtq, 2dea – VpLeu-AP – Vibrio proteolyticus
    
  • 3b35, 3b3t, 3b3v, 2anp - VpLeu-AP (mutant)
    
  • 3b3c, 3b3s, 3b3w - VpLeu-AP (mutant)+Leu derivative
    
  • 3b7i - VpLeu-AP (mutant)+Leu
    
  • 1ft7 - VpLeu-AP +Leu derivative
    
  • 3vh9 - VpLeu-AP + 8-quinolinol
    
  • 2nyq, 2iq6 – VpLeu-AP+polypeptide
    
  • 1lok – VpLeu-AP+Tris
    
  • 2prq – VpLeu-AP+Co
    
  • 1xry, 1txr – VpLeu-AP+bestatin
    
  • 1gyt – EcLeu-AP
    
  • 3t8w, 4k3n, 4r6t – PfLeu-AP + Zn + inhibitor
    
  • 4r76, 4r7m, 4x2t – PfLeu-AP (mutant) + Zn + inhibitor
    
  • 3tc8 - PdLeu-AP + Zn
    
  • 4fuu - Leu-AP + Zn – Bacterioides thetaiotaomicron
    
  • 4ksi – toLeu-AP 1 + Mg – tomato
    
  • 5d8n – toLeu-AP 1 (mutant) + Mg
    
  • 5lhj – StrLeu-AP 2 – Streptomyces
    
  • 5lhk – StrLeu-AP 2 + Mn
    
  • 4zla, 4zi6 – Leu-AP + Zn – Helicobacter pylori
    

• Leucine-cysteine aminopeptidase

• • 4p8q, 5c97 – hLeu-Cys-AP + Zn
    
  • 4pj6 – hLeu-Cys-AP + Zn + lysine
    

• • 4z7i – hLeu-Cys-AP + Zn + peptide
    

• Lysine aminopeptidase

• • 4x8i – PfLys-AP + Zn
    

• Methionine aminopeptidase

• • 3mr1, 3mx6 – Met-AP+Mn – Rickettsia prowazekii
    
  • 2dfi, 1xgm, 1xgn, 1xgo, 1xgs – PyfMet-AP+Co – Pyrococcus furiosus
    
  • 1wkm - PyfMet-AP+Mn
    
  • 4fo7, 4juq - PaMet-AP+Mn – Pseudomonas aeruginosa
    
  • 4fo8 - PaMet-AP+Mn + Met
    
  • 4hxx, 4iu6 - hMet-AP 1 + Co + pyrimidine derivative
    
  • 2nq6, 2nq7, 1yw7, 1yw8, 1yw9 - hMet-AP 1 +Mn+inhibitor
    
  • 2b3h, 2b3k - hMet-AP 1 +Co
    
  • 2gz5, 4ikr, 4iks, 4ikt, 4iku – hMet-AP 1 +Co+inhibitor
    
  • 2g6p - hMet-AP 1 truncated+Mn+inhibitor
    
  • 2ea2, 2ea4, 2ga2 - hMet-AP 2 +Mn+inhibitor
    
  • 1boa - hMet-AP 2 +Co+ angiogenesis inhibitor
    
  • 1kq0, 1kq9 – hMet-AP 2 +methionine
    
  • 1qzy, 1b59, 1b6a, 1bn5, 2oaz, 5d6f, 5d6e - hMet-AP 2 +Co+inhibitor
    
  • 2adu - hMet-AP 2 (mutant) +Co+inhibitor
    
  • 1r58, 1r5g, 1r5h - hMet-AP 2 +Mn+inhibitor
    
  • 3iu7 – MtMet-AP+Mn +A02 – Mycobacterium tuberculosis
    
  • 3iu8, 3iu9 - MtMet-AP+Ni + inhibitor
    
  • 1yj3, 3ror, 4ook - MtMet-AP 2 +Co
    
  • 3pka - MtMet-AP+Mn
    
  • 3pkb, 3pkc, 3pkd, 3pke - MtMet-AP+bengamide inhibitor
    
  • 3tav – Met-AP + Mg – Mycobacterium abscessus< br />
  • 1y1n - MtMet-AP+K
    
  • 4idy, 4iec - MtMet-AP+K + hydroxyethyl disulfide
    
  • 4if7 - MtMet-AP+K + homocysteinemethyl disulfide
    
  • 3fm3 – EncMet-AP – Encephalitozoon cuniculi
    
  • 3fmq, 3fmr - EncMet-AP+angiogenesis inhibitor
    
  • 3d27, 2q92, 2q93, 2q94, 2q95, 2q96, 2p98, 2p99, 2p9a, 2gu4, 2gu5, 2gu6, 2evc, 2evm, 2evo, 2bbv, 1xnz, 4a6v, 4a6w, 2bb7 – EcMet-AP+Mn+inhibitor
    
  • 2gg0, 2gg2, 2gg3, 2gg5, 2gg7, 2gg8, 2gg9, 2ggb, 2ggc, 4pnc - EcMet-AP+Co+inhibitor
    
  • 1c21, 1c22, 1c23, 1c24 - EcMet-AP +Co + methionine derivative
    
  • 1c27 - EcMet-AP +Co +norleucine
    
  • 3tb5 – Met-AP – Enterococcus faecalis
    
  • 2gtx, 2gu7 – EcMet-AP
    
  • 1yvm – EcMet-AP (mutant)+Co+thiabendazole
    
  • 1mat – EcMet-AP+Co
    
  • 2mat, 4mat, 4u76, 4u75, 4u73, 4u71, 4u70, 4u6z, 4u6w, 4u6j, 4u6e, 4u6c, [[4u769], 4u1b - EcMet-AP 1 (mutant)+Co
    
  • 3mat - EcMet-AP (mutant)+Co+bestatin derivative
    
  • 4fli, 4flj, 4flk, 4fll - hMet-AP 1 +Mn+inhibitor
    
  • 1qxw, 1qxy, 1qxz – Met-AP+Co+inhibitor - Staphylococcus aureus
    
  • 1o0x – TmMet-AP
    
  • 3s6b – PfMet-AP + Fe
    
  • 4fuk – TbMet-AP + Zn – Trypanosoma brucei
    
  • 4km3 – SpAP
    

• Arginine aminopeptidase

• • 5cu5 – hArg-AP 2
    
  • 4jbs – hArg-AP 2 + Zn + inhibitor
    
  • 5ab2, 5ab0 – hArg-AP 2 + Zn + peptide
    

• Aspartic acid aminopeptidase

• • 4dyo – hAsp-AP+aspartic hydroxamate
    
  • 3var, 3vat – bAsp-AP
    
  • 4eme – PfAsp-AP + Zn

• Asparagine aminopeptidase

• • 3c17, 2zak – EcAsn-AP (mutant)
    
  • 2zal – EcAsn-AP+Asp
    
  • 2gez – Asn-AP – Lupinus luteus

• Serine aminopeptidase

• • 1b65 – OaSer-AP – Ochrobactrum anthropi

• Cytosolic aminopeptidase

• • 3pei – FtCyt-AP
    
  • 3kzw – Cyt-AP – Staphylococcus aureus
    
  • 3ij3 – Cyt-AP – Coxiella burnetii

• Aminopeptidase 2

• • 3se6 – hAPN
    
  • 4e36 – hAPN + Zn

• Non-specific aminopeptidase

• • 2ek8 – AnAP – Aneurinibacillus
    
  • 2ek9 – AnAP+bestatin
    
  • 1y0r, 1xfo – PhAP
    
  • 1y0y – PhAP+amastatin
    
  • 1amp - VpAP
    
  • 1cp6, 1igb – VpAP+inhibitor
    
  • 1ei5 – OaAP
    
  • 3edy, 3ee6 – hTripeptidyl-AP
    
  • 3zn8 – Dipeptidyl-AP B + signal recognition particle protein + signal recognition particle receptor + RNA – yeast
    
  • 4efd – TbAP M17 + Mn
    
  • 4fgm – AP N + Zn – Idiomarina loihiensis
    
  • 4icq – SpAP Peps + Zn
    
  • 4icr – SpAP Peps (mutant) + Zn
    
  • 4ics – SpAP Peps (mutant) + Zn + Trp + Gly
    
  • 4pu2, 4pvb – NmAP N + Leu analog
    
  • 4pw4 – NmAP N + Phe analog
    
  • 4qhp, 4qir, 4qme, 4qpe, 4quo – NmAP N + dipeptide analog
    
  • 4wwv – AP M42 – Desulfuroccus kamchatkensis
    
  • 4p6y – TmAP M42
    

• Cold-activated aminopeptidase

• • 3cia – Col-AP – Colwellia psychrerythraea

• Deblocking aminopeptidase

• • 2gre – DAP – Bacillus cereus

• Heat stable aminopeptidase

• • 2ayi – AmpT – Thermus thermophilus

• Aminopeptidase from Staphylococcus aureus

• • 1zjc - AmpS

• Metalloaminopeptidase

• • 3q43, 3q44 – PfPFAP (mutant) + bestatin derivative
    

• Stereomyces griesus aminopeptidase

• • 1xjo, 1cp7 - SGAP
    
  • 1qq9, 1f2o, 1f2p, 1tf8, 1tf9, 1tkf, 1tkh, 1tkj, 1xbu - SGAP + amino acid

• β-peptidyl aminopeptidase

• • 3n2w – SxBapA – Sphingosinicella xenopeptidilytica
    
  • 3n5i – SxBapA (mutant)
    
  • 3n33 – SxBapA + AEBSF
    
  • 3ndv, 3nfb – SxBapA + ampicillin

• M1 family aminopeptidase

• • 4j3b – PfAP (mutant)
    
  • 3t8v – PfAP M1
    
  • 4k5l, 4k5m, 4k5n, 4k5p, 4k5o, 5cbm - PfLeu-AP (mutant) + Zn + inhibitor
    
  • 4zx6, 4zx5, 4zx4, 4zx5, 4zx3, 4zw8, 4zw7, 4zw6, 4zw5, 4zw3, 4zqt, 4x2u - PfLeu-AP (mutant) + Zn + Mg + inhibitor
    

• Aminopeptidase C

• • 4k7c – AP – Lactobacillus rahmnosis
    
  • 5ib9 – AP - Aneurinibacillus
    

• Tripeptidyl aminopeptidase see Tripeptidyl peptidase

• Dipeptidyl aminopeptidase see Dipeptidyl peptidase

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Additional Resources

For additional information, see:
Amino Acid Synthesis & Metabolism
Streptomyces griseus Aminopeptidase (SGAP)

References

1. ↑ Taylor A. Aminopeptidases: structure and function. FASEB J. 1993 Feb 1;7(2):290-8. PMID:8440407
2. ↑ Hanaya K, Suetsugu M, Saijo S, Yamato I, Aoki S. Potent inhibition of dinuclear zinc(II) peptidase, an aminopeptidase from Aeromonas proteolytica, by 8-quinolinol derivatives: inhibitor design based on Zn(2+) fluorophores, kinetic, and X-ray crystallographic study. J Biol Inorg Chem. 2012 Feb 5. PMID:22311113 doi:10.1007/s00775-012-0873-4