Aminopeptidase P

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William H. Simmons - One of the best experts on this subject based on the ideXlab platform.

  • AminoPePtidase P isozyme exPression in human tissues and PeriPheral blood mononuclear cell fractions
    Archives of Biochemistry and Biophysics, 2005
    Co-Authors: Cagatay Ersahin, Arthur T. Orawski, Anna M Szpaderska, William H. Simmons
    Abstract:

    Abstract AminoPePtidase P (APP) isoforms sPecifically remove the N-terminal amino acid from PePtides that have a Proline residue in the second Position. The mRNA levels of three different isoforms, each coded by a different gene, were determined in 16 human tissues and in PeriPheral blood mononuclear cell (PBMC) fractions by RT-PCR. The cytosolic isoform, APP1, and the cell surface membrane-bound isoform, APP2, are exPressed in all of the human tissues and PBMC fractions examined. The very high exPression of APP2 mRNA in kidney comPared to other tissues was confirmed by enzyme activity measurements. Among the PBMC fractions, APP2 exPression is highest in resting CD8 + T cells, but decreases in these cells following their activation with Phytohemagglutinin; in contrast, exPression of APP2 increases in CD4 + T cells uPon activation. The third isoform, APP3, is a hyPothetical Protein identified by nucleotide sequencing. A detailed analysis of its amino acid sequence confirmed that the Protein is an AminoPePtidase P-like enzyme with greater similarity to Escherichia coli APP than to either APP1 or APP2. Two sPlice variants of APP3 exist, one of which is Predicted to have a mitochondrial localization (APP3m) while the other is cytosolic (APP3c). Both forms are variably exPressed in all of the human tissues and PBMC fractions examined.

  • human recombinant membrane bound AminoPePtidase P Production of a soluble form and characterization using novel internally quenched fluorescent substrates
    Biochemical Journal, 2005
    Co-Authors: Giuseppe Molinaro, William H. Simmons, Yves Lepage, Adriana K Carmona, Maria A Juliano, Luiz Juliano, Elena Malitskaya, Marieandree Yessine, Miguel Chagnon, Guy Boileau
    Abstract:

    APP (AminoPePtidase P) has the unique ability to cleave the N-terminal amino acid residue from PePtides exhibiting a Proline at P1′. DesPite its Putative involvement in the Processing of bioactive PePtides, among them the kinins, little is known about the Physiological roles of both human forms of APP. The PurPose of the Present study is first to engineer and characterize a secreted form of hmAPP (human membrane-bound APP). Our biochemical analysis has shown that the exPressed glycosylated Protein is fully functional, and exhibits enzymic Parameters similar to those described Previously for mAPP Purified from Porcine or bovine lungs or exPressed from a Porcine clone. This soluble form of hmAPP cross-reacts with a Polyclonal antiserum raised against a 469-amino-acid hmAPP fragment Produced in Escherichia coli. Secondly, we synthesized three internally quenched fluorescent PePtide substrates that exhibit a similar affinity for the enzyme than its natural substrates, the kinins, and a higher affinity comPared with the triPePtide Arg-Pro-Pro used until now for the quantification of APP in biological samPles. These new substrates rePresent a helPful analytical tool for raPid and reliable screening of Patients suscePtible to adverse reactions associated with angiotensin-converting enzyme inhibitors or novel vasoPePtidase (mixed angiotensin-converting enzyme/nePrilysin) inhibitors.

  • structure of escherichia coli AminoPePtidase P in comPlex with the inhibitor aPstatin
    Acta Crystallographica Section D-biological Crystallography, 2004
    Co-Authors: S C Graham, William H. Simmons, Megan J Maher, H C Freeman, Mitchell J Guss
    Abstract:

    AminoPePtidase P (APPro) is a metalloProtease whose active site includes a dinuclear manganese(II) cluster. The enzyme cleaves the N-terminal residue from a PolyPePtide when the second residue is Proline. A comPlex of Escherichia coli APPro (EcAPPro) with an inhibitor, aPstatin [N-(2S,3R)-3-­amino-2-hydroxy-4-Phenyl-butanoyl-l-Prolyl-l-Prolyl-l-alaninamide], has been crystallized. APstatin binds to the active site of EcAPPro with its N-terminal amino grouP coordinated to one of the two MnII atoms at the metal centre. The aPstatin hydroxyl grouP rePlaces a hydroxide ion which bridges the two metal atoms in the native enzyme. The first Proline residue of aPstatin lies in a small hydroPhobic cleft. The structure of the aPstatin–EcAPPro comPlex has been refined at 2.3 A resolution with residuals R = 0.179 and Rfree = 0.204. The structure of the comPlex illustrates how aPstatin inhibits APPro and suggests how substrates may bind to the enzyme, but the basis of the Proline-sPecificity remains elusive.

  • rat and mouse membrane AminoPePtidase P structure analysis and tissue distribution
    Archives of Biochemistry and Biophysics, 2003
    Co-Authors: Cagatay Ersahin, Anna M Szpaderska, William H. Simmons
    Abstract:

    Abstract Membrane-bound AminoPePtidase P (mAPP) is a highly sPecific exoPePtidase that removes the N-terminal amino acid only from a PePtide (three amino acids or longer) that has a Prolyl residue in the second Position. mAPP can inactivate bradykinin, a Potent vasodilating and cardioProtective PePtide hormone, by hydrolyzing the Arg1–Pro2 bond. Studies on the rat have shown that the metabolism of bradykinin is an imPortant Physiological role of this enzyme. We rePort here the comPlete coding sequences for rat and mouse mAPP determined from mRNA isolated from lung tissue. Key structural features that determine Post-translational Processing and substrate recognition and catalysis were identified based on sequence homologies and the crystal structure of Escherichia coli AminoPePtidase P comPlexed with Pro–Leu. The tissue-sPecific exPression of mAPP was studied using the Polymerase chain reaction. The mAPP gene is widely, but variably, exPressed in adult tissues of the rat and mouse and in mouse embryos.

  • Inhibitors of the bradykinin-degrading enzyme, AminoPePtidase P
    Peptides for the New Millennium, 2002
    Co-Authors: William H. Simmons, Arthur T. Orawski, Linda L. Maggiora
    Abstract:

    AminoPePtidase P inactivates bradykinin by hydrolyzing the bond [1]. This enzyme is a metallo-AminoPePtidase with sPecificity for Proline in the Penultimate Position. An inhibitor of this enzyme was synthesized and called aPstatin (N-[(2S,3R)-3amino-2-hydroxy-4-Phenylbutanoyl]-L-Pro-L-Pro-L-Ala-NH2) [2]. The N-terminal residue of aPstatin was designed to chelate the active site through the amino and hydroxyl functions. The remaining residues were designed to accommodate the Primary and secondary sPecificity requirements. APstatin has an of for human membranebound AminoPePtidase P. APstatin together with an angiotensin converting enzyme inhibitor can comPletely block bradykinin degradation in the rat Pulmonary and coronary circulations [2,3]. APstatin can Potentiate the vasodePressor resPonse to intravenously-administered bradykinin and can reduce blood Pressure in rats made hyPertensive by aortic coarctation [4]. APstatin can also significantly reduce cardiac ischemia/rePerfusion damage as well as decrease rePerfusion-induced ventricular fibrillation in the isolated rat heart [5]. The antihyPertensive and cardioProtective effects of aPstatin are blocked by a bradykinin recePtor antagonist, suggesting that aPstatin’s effects are due to Potentiation of endogenously-formed bradykinin. In order to delineate the structural requirements for AminoPePtidase P inhibition, 15 aPstatin analogs were synthesized and tested for their ability to inhibit membrane-bound AminoPePtidase P from human, monkey, rat, and bovine lung. Data for the human enzyme are described.

Anthony J Turner - One of the best experts on this subject based on the ideXlab platform.

  • The bradykinin-degrading AminoPePtidase P is increased in women taking the oral contracePtive Pill
    Journal of the Renin-Angiotensin-Aldosterone System, 2008
    Co-Authors: Amy L. Cilia La Corte, Anthony J Turner, Angela M. Carter, Peter J. Grant, Nigel M Hooper
    Abstract:

    Introduction.The renin-angiotensin and kininogen-kinin hormonal systems are critically involved in regulating blood Pressure and are candidates in contributing to oral contracePtive Pill (OCP)-induced hyPertension. Angiotensinconverting enzyme (ACE) and AminoPePtidase P (AP-P) are key enzymes in these systems and are both involved in the degradation of the vasodilator bradykinin. Methods. Circulating ACE and AP-P levels were measured by activity assay using selective fluorogenic PePtide substrates in Plasma samPles from the Leeds Family Study. In addition, the effect of Progesterone on the exPression of AP-P and ACE was examined in cells. Results.Women on the OCP had higher ageadjusted Plasma AP-P (mean [95% confidence interval]) (0.27 [0.23-0.32] nmol/min/ml (n = 53)) comPared with women not on the OCP (0.17 [0.16-0.19] nmol/min/ml (n = 133), P < 0.001) or males (0.19 [0.17-0.20] nmol/min/ml (n = 209), P

  • the bradykinin degrading AminoPePtidase P is increased in women taking the oral contracePtive Pill
    Journal of the Renin-Angiotensin-Aldosterone System, 2008
    Co-Authors: Amy L. Cilia La Corte, Anthony J Turner, Angela M. Carter, Peter J. Grant, Nigel M Hooper
    Abstract:

    Introduction.The renin-angiotensin and kininogen-kinin hormonal systems are critically involved in regulating blood Pressure and are candidates in contributing to oral contracePtive Pill (OCP)-induced hyPertension. Angiotensinconverting enzyme (ACE) and AminoPePtidase P (AP-P) are key enzymes in these systems and are both involved in the degradation of the vasodilator bradykinin. Methods. Circulating ACE and AP-P levels were measured by activity assay using selective fluorogenic PePtide substrates in Plasma samPles from the Leeds Family Study. In addition, the effect of Progesterone on the exPression of AP-P and ACE was examined in cells. Results.Women on the OCP had higher ageadjusted Plasma AP-P (mean [95% confidence interval]) (0.27 [0.23-0.32] nmol/min/ml (n = 53)) comPared with women not on the OCP (0.17 [0.16-0.19] nmol/min/ml (n = 133), P < 0.001) or males (0.19 [0.17-0.20] nmol/min/ml (n = 209), P <0.001). There were no differences in the age-adjusted Plasma ACE levels among the three grouPs. In HePG2 cells, Progesterone treatment increased the AP-P Protein and mRNA exPression, whereas no effect of Progesterone treatment was observed for ACE. Conclusion. Increased AP-P may result in increased breakdown of bradykinin. These data suggest that Progesterone-induced increases in AP-P may contribute to the develoPment of OCP-induced hyPertension in suscePtible Women.

  • identification of critical residues in the active site of Porcine membrane bound AminoPePtidase P
    Biochemistry, 2000
    Co-Authors: Graeme S Cottrell, Nigel M Hooper, Ralph J Hyde, Mark R Parsons, Anthony J Turner
    Abstract:

    The membrane-bound form of mammalian AminoPePtidase P (AP-P; EC 3.4. 11.9) is a mono-zinc-containing enzyme that lacks any of the tyPical metal binding motifs found in other zinc metalloProteases. To identify residues involved in metal binding and catalysis, sequence and structural information was used to align the sequence of Porcine membrane-bound AP-P with other members of the PePtidase clan MG, including Escherichia coli AP-P and methionyl AminoPePtidases. Residues Predicted to be critical for activity were mutated and the resultant Proteins were exPressed in COS-1 cells. ImmunoelectroPhoretic blot analysis was used to comPare the levels of exPression of the mutant Proteins, and their ability to hydrolyze bradykinin and Gly-Pro-hydroxyPro was assessed. AsP449, AsP460, His523, Glu554, and Glu568 are Predicted to serve as metal ion ligands in the active site, and mutagenesis of these residues resulted in fully glycosylated Proteins that were catalytically inactive. Mutation of His429 and His532 also resulted in catalytically inactive Proteins, and these residues, by analogy with E. coli AP-P, are likely to Play a role in shuttling Protons during catalysis. These studies indicate that mammalian membrane-bound AP-P has an active-site configuration similar to that of other members of the PePtidase clan MG, which is comPatible with either a dual metal ion model or a single metal ion in the active site. The latter model is consistent, however, with the known metal stoichiometry of both the membrane-bound and cytosolic forms of AP-P and with a recently ProPosed model for methionyl AminoPePtidase.

  • cloning exPression and characterization of human cytosolic AminoPePtidase P a single manganese ii dePendent enzyme
    Biochemistry, 2000
    Co-Authors: Graeme S Cottrell, Nigel M Hooper, Anthony J Turner
    Abstract:

    The mammalian bradykinin-degrading enzyme AminoPePtidase P (AP-P; E. C. 3.4.11.9) is a metal-dePendent enzyme and is a member of the PePtidase clan MG. AP-P exists as membrane-bound and cytosolic forms, which rePresent distinct gene Products. A Partially truncated clone encoding the cytosolic form was obtained from a human Pancreatic cDNA library and the 5' region containing the initiating Met was obtained by 5' raPid accumulation of cDNA ends (RACE). The oPen reading frame encodes a Protein of 623 amino acids with a calculated molecular mass of 69,886 Da. The full-length cDNA with a C-terminal hexahistidine tag was exPressed in Escherichia coli and COS-1 cells and migrated on SDS-PAGE with a molecular mass of 71 kDa. The exPressed cytosolic AP-P hydrolyzed the X-Pro bond of bradykinin and substance P but did not hydrolyze Gly-Pro-hydroxyPro. Hydrolysis of bradykinin was inhibited by 1,10-Phenanthroline and by the sPecific inhibitor of the membrane-bound form of mammalian AP-P, aPstatin. Inductively couPled Plasma atomic emission sPectroscoPy of AP-P exPressed in E. coli revealed the Presence of 1 mol of manganese/mol of Protein and insignificant amounts of cobalt, iron, and zinc. The enzymatic activity of AP-P was Promoted in the Presence of Mn(II), and this activation was increased further by the addition of glutathione. The only other metal ion to cause slight activation of the enzyme was Co(II), with Ca(II), Cu(II), Mg(II), Ni(II), and Zn(II) all being inhibitory. Removal of the metal ion from the Protein was achieved by treatment with 1,10-Phenanthroline. The metal-free enzyme was reactivated by the addition of Mn(II) and, Partially, by Fe(II). Neither Co(II) nor Zn(II) reactivated the metal-free enzyme. On the basis of these data we ProPose that human cytosolic AP-P is a single metal ion-dePendent enzyme and that manganese is most likely the metal ion used in vivo.

  • evaluation of some fluorogenic substrates for continuous assay of AminoPePtidase P
    Analytical Biochemistry, 1997
    Co-Authors: Susan Hawthorne, Anthony J Turner, Patrick Harriott, Brian Walker, Carvell H Williams
    Abstract:

    Abstract Three Potential fluorogenic substrates for assay of AminoPePtidase P (AP-P) have been PrePared and evaluated, using enzyme Purified from Porcine kidney. They are based on internal quenching of the synthetic, fluorescent amino acid ( R,S )-2-amino-3-(7-methoxy4-coumaryl)ProPanoic acid (( R,S )-AmP) by a 2,4dinitroPhenyl (DNP) grouP. The comPounds are X-Pro-Pro-( R,S )-AmP-NH 2 , where X is H-Lys(ϵ-DNP), H-Orn(δ-DNP), or L-2-amino-3-(DNP)aminoProPionic acid. The first two were found to be excellent substrates for AP-P, with resPective K m values of 4.8 and 5.2 μ m . An advantageous feature is that under the conditions of assay, using 4-mm 2 cells, the substrates are without noticeable quenching effect on the fluorescence of Pro-Pro-( R,S )-AmP-NH 2 (the Product liberated by the action of AP-P). At concentrations greater than about 30–50 μ m , both substrates aPPear to inhibit the enzyme, but this has little Practical consequence since assays can be carried out at substrate concentrations, giving uP to aPProximately 80% of V max without this inhibitory effect being noticeable. The Lys derivative was found to be a very useful substrate for a continuous assay for AP-P and equally good in a discontinuous assay of multiPle samPles using microtiter Plates. The racemic center at the AmP residue did not Prevent total hydrolysis of the Lys derivative, suggesting that subsite sPecificity in AP-P does not extend as far as the P3′ Position.

J J Powell - One of the best experts on this subject based on the ideXlab platform.

Nigel M Hooper - One of the best experts on this subject based on the ideXlab platform.

  • a functional xPnPeP2 Promoter haPlotyPe leads to reduced Plasma AminoPePtidase P and increased risk of ace inhibitor induced angioedema
    Human Mutation, 2011
    Co-Authors: Amy Cilia L La Corte, Albert Adam, Angela M. Carter, Peter J. Grant, Gillian I Rice, Qing Ling Duan, Guy A Rouleau, Nigel M Hooper
    Abstract:

    Angiotensin I-converting enzyme inhibitors (ACEi) are widely used antihyPertensive agents that are associated with a Potentially life-threatening reaction, ACEi-angioedema. ImPaired metabolism of bradykinin and des-Arg(9) -bradykinin by AminoPePtidase P (APP) is a key contributor to ACEi-angioedema. This study aimed to characterize the genetic regulation of the XPNPEP2 gene and identify the genetic factors contributing to variance in Plasma APP activity and ACEi-angioedema. Additive genetic factors accounted for 47.3% of variance in Plasma APP activity in healthy individuals. Nested deletion analysis identified the minimal Promoter (-338 bP to -147 bP) and an enhancer region (-2,502 bP to -2,238 bP). Three PolymorPhisms (c.-2399C>A, c.-1612G>T, and c.-393G>A) were significantly associated with Plasma APP activity. HaPlotyPe ATG was significantly associated with reduced rePorter gene activity and with reduced Plasma APP activity. The c.-2399C>A PolymorPhism was located in an enhancer region and was Predicted to differentially bind hePatic nuclear factor 4 (HNF4). Over exPression of HNF4 increased the activation of haPlotyPe ATG comPared with haPlotyPe CGG. In a case control study of subjects with a history of ACEi-angioedema, haPlotyPe ATG was significantly associated with ACEi-angioedema (OR 4.87 [1.78-13.35] P = 0.002). The ATG haPlotyPe is functional and contributes to ACEi-angioedema through a reduction in APP. Hum Mutat 32:1326-1331, 2011. (c)2011 Wiley Periodicals, Inc.

  • A functional XPNPEP2 Promoter haPlotyPe leads to reduced Plasma AminoPePtidase P and increased risk of ACE inhibitor‐induced angioedema
    Human Mutation, 2011
    Co-Authors: Amy L. Cilia La Corte, Albert Adam, Angela M. Carter, Peter J. Grant, Gillian I Rice, Qing Ling Duan, Guy A Rouleau, Nigel M Hooper
    Abstract:

    Angiotensin I-converting enzyme inhibitors (ACEi) are widely used antihyPertensive agents that are associated with a Potentially life-threatening reaction, ACEi-angioedema. ImPaired metabolism of bradykinin and des-Arg(9) -bradykinin by AminoPePtidase P (APP) is a key contributor to ACEi-angioedema. This study aimed to characterize the genetic regulation of the XPNPEP2 gene and identify the genetic factors contributing to variance in Plasma APP activity and ACEi-angioedema. Additive genetic factors accounted for 47.3% of variance in Plasma APP activity in healthy individuals. Nested deletion analysis identified the minimal Promoter (-338 bP to -147 bP) and an enhancer region (-2,502 bP to -2,238 bP). Three PolymorPhisms (c.-2399C>A, c.-1612G>T, and c.-393G>A) were significantly associated with Plasma APP activity. HaPlotyPe ATG was significantly associated with reduced rePorter gene activity and with reduced Plasma APP activity. The c.-2399C>A PolymorPhism was located in an enhancer region and was Predicted to differentially bind hePatic nuclear factor 4 (HNF4). Over exPression of HNF4 increased the activation of haPlotyPe ATG comPared with haPlotyPe CGG. In a case control study of subjects with a history of ACEi-angioedema, haPlotyPe ATG was significantly associated with ACEi-angioedema (OR 4.87 [1.78-13.35] P = 0.002). The ATG haPlotyPe is functional and contributes to ACEi-angioedema through a reduction in APP. Hum Mutat 32:1326-1331, 2011. (c)2011 Wiley Periodicals, Inc.

  • The bradykinin-degrading AminoPePtidase P is increased in women taking the oral contracePtive Pill
    Journal of the Renin-Angiotensin-Aldosterone System, 2008
    Co-Authors: Amy L. Cilia La Corte, Anthony J Turner, Angela M. Carter, Peter J. Grant, Nigel M Hooper
    Abstract:

    Introduction.The renin-angiotensin and kininogen-kinin hormonal systems are critically involved in regulating blood Pressure and are candidates in contributing to oral contracePtive Pill (OCP)-induced hyPertension. Angiotensinconverting enzyme (ACE) and AminoPePtidase P (AP-P) are key enzymes in these systems and are both involved in the degradation of the vasodilator bradykinin. Methods. Circulating ACE and AP-P levels were measured by activity assay using selective fluorogenic PePtide substrates in Plasma samPles from the Leeds Family Study. In addition, the effect of Progesterone on the exPression of AP-P and ACE was examined in cells. Results.Women on the OCP had higher ageadjusted Plasma AP-P (mean [95% confidence interval]) (0.27 [0.23-0.32] nmol/min/ml (n = 53)) comPared with women not on the OCP (0.17 [0.16-0.19] nmol/min/ml (n = 133), P < 0.001) or males (0.19 [0.17-0.20] nmol/min/ml (n = 209), P

  • the bradykinin degrading AminoPePtidase P is increased in women taking the oral contracePtive Pill
    Journal of the Renin-Angiotensin-Aldosterone System, 2008
    Co-Authors: Amy L. Cilia La Corte, Anthony J Turner, Angela M. Carter, Peter J. Grant, Nigel M Hooper
    Abstract:

    Introduction.The renin-angiotensin and kininogen-kinin hormonal systems are critically involved in regulating blood Pressure and are candidates in contributing to oral contracePtive Pill (OCP)-induced hyPertension. Angiotensinconverting enzyme (ACE) and AminoPePtidase P (AP-P) are key enzymes in these systems and are both involved in the degradation of the vasodilator bradykinin. Methods. Circulating ACE and AP-P levels were measured by activity assay using selective fluorogenic PePtide substrates in Plasma samPles from the Leeds Family Study. In addition, the effect of Progesterone on the exPression of AP-P and ACE was examined in cells. Results.Women on the OCP had higher ageadjusted Plasma AP-P (mean [95% confidence interval]) (0.27 [0.23-0.32] nmol/min/ml (n = 53)) comPared with women not on the OCP (0.17 [0.16-0.19] nmol/min/ml (n = 133), P < 0.001) or males (0.19 [0.17-0.20] nmol/min/ml (n = 209), P <0.001). There were no differences in the age-adjusted Plasma ACE levels among the three grouPs. In HePG2 cells, Progesterone treatment increased the AP-P Protein and mRNA exPression, whereas no effect of Progesterone treatment was observed for ACE. Conclusion. Increased AP-P may result in increased breakdown of bradykinin. These data suggest that Progesterone-induced increases in AP-P may contribute to the develoPment of OCP-induced hyPertension in suscePtible Women.

  • identification of critical residues in the active site of Porcine membrane bound AminoPePtidase P
    Biochemistry, 2000
    Co-Authors: Graeme S Cottrell, Nigel M Hooper, Ralph J Hyde, Mark R Parsons, Anthony J Turner
    Abstract:

    The membrane-bound form of mammalian AminoPePtidase P (AP-P; EC 3.4. 11.9) is a mono-zinc-containing enzyme that lacks any of the tyPical metal binding motifs found in other zinc metalloProteases. To identify residues involved in metal binding and catalysis, sequence and structural information was used to align the sequence of Porcine membrane-bound AP-P with other members of the PePtidase clan MG, including Escherichia coli AP-P and methionyl AminoPePtidases. Residues Predicted to be critical for activity were mutated and the resultant Proteins were exPressed in COS-1 cells. ImmunoelectroPhoretic blot analysis was used to comPare the levels of exPression of the mutant Proteins, and their ability to hydrolyze bradykinin and Gly-Pro-hydroxyPro was assessed. AsP449, AsP460, His523, Glu554, and Glu568 are Predicted to serve as metal ion ligands in the active site, and mutagenesis of these residues resulted in fully glycosylated Proteins that were catalytically inactive. Mutation of His429 and His532 also resulted in catalytically inactive Proteins, and these residues, by analogy with E. coli AP-P, are likely to Play a role in shuttling Protons during catalysis. These studies indicate that mammalian membrane-bound AP-P has an active-site configuration similar to that of other members of the PePtidase clan MG, which is comPatible with either a dual metal ion model or a single metal ion in the active site. The latter model is consistent, however, with the known metal stoichiometry of both the membrane-bound and cytosolic forms of AP-P and with a recently ProPosed model for methionyl AminoPePtidase.

S J Hope - One of the best experts on this subject based on the ideXlab platform.

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