Carboxypeptidase A

Handbook of Proteolytic Enzymes

Volumn 1, Issue , 2013, Pages 1289-1301

  Auld, David S ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84884846158     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-382219-2.00290-8     Document Type: Chapter

References (126)

1. Anson M.L. Carboxypeptidase: I. The preparation of crystalline carboxypeptidase. J. Gen. Physiol. 1937, 20(5):663-669.
2. Vallee B.L., Neurath H. Carboxypeptidase, a zinc metalloenzyme. J. Biol. Chem. 1955, 217(1):253-261.
3. Davies R.C., Auld D.S., Vallee B.L. The effect of modifiers on the hydrolysis of esters and peptides by carboxypeptidase A. Biochem. Biophys. Res. Commun. 1968, 31(4):628-633.
4. Davies R.C., Riordan J.F., Auld D.S., Vallee B.L. Kinetics of carboxypeptidase A. I. Hydrolysis of carbobenzoxyglycyl-l-phenylalanine, benzoylglycyl-l-phenylalanine, and hippuryl-d,l-beta-phenyllactic acid by metal-substituted and acetylated carboxypeptidases. Biochemistry 1968, 7(3):1090-1099.
5. Auld D.S., Vallee B.L. Kinetics of carboxypeptidase A. II. Inhibitors of the hydrolysis of oligopeptides. Biochemistry 1970, 9(3):602-609.
6. Auld D.S., Vallee B.L. Kinetics of carboxypeptidase A, pH and temperature dependence of tripeptide hydrolysis. Biochemistry 1971, 10(15):2892-2897.
7. Peterson L.M., Holmquist B., Bethune J.L. A unique activity assay for carboxypeptidase A in human serum. Anal. Biochem. 1982, 125(2):420-426.
8. Latt S.A., Auld D.S., Vallee B.L. Fluorescence determination of carboxypeptidase A activity based on electronic energy transfer. Anal. Biochem. 1972, 50(1):56-62.
9. Ng M., Auld D.S. A fluorescent oligopeptide energy transfer assay with broad applications for neutral proteases. Anal. Biochem. 1989, 183(1):50-56.
10. Guasch A., Coll M., Aviles F.X., Huber R. Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation. J. Mol. Biol. 1992, 224(1):141-157.
11. Phillips M.A., Rutter W.J. Role of the prodomain in folding and secretion of rat pancreatic carboxypeptidase A1. Biochemistry 1996, 35(21):6771-6776.
12. Vendrell J., Querol E., Aviles F.X. Metallocarboxypeptidases and their protein inhibitors. Structure, function and biomedical properties. Biochim. Biophys. Acta. 2000, 1477(1-2):284-298.
13. Gomis-Ruth F.X., Gomez-Ortiz M., Vendrell J., Ventura S., Bode W., Huber R., Aviles F.X. Crystal structure of an oligomer of proteolytic zymogens: detailed conformational analysis of the bovine ternary complex and implications for their activation. J. Mol. Biol. 1997, 269(5):861-880.
14. Behnke W.D., Vallee B.L. The spectrum of cobalt bovine procarboxypeptidase A, an index of catalytic function. Proc. Natl. Acad. Sci. USA 1972, 69(9):2442-2445.
15. Rees D.C., Lewis M., Lipscomb W.N. Refined crystal structure of carboxypeptidase A at 1.54 Å resolution. J. Mol. Biol. 1983, 168(2):367-387.
16. Neurath H. Evolution of proteolytic enzymes. Science 1984, 224(4647):350-357.
17. Vendrell J., Guasch A., Coll M., Villegas V., Billeter M., Wider G., Huber R., Wuthrich K., Aviles F.X. Pancreatic procarboxypeptidases: their activation processes related to the structural features of the zymogens and activation segments. Biol. Chem. Hoppe Seyler 1992, 373(7):387-392.
18. Vendrell J., Aviles F.X., Fricker L.D. Metallocarboxypeptidases. The Handbook of Metalloproteins 2004, Vol. 3:176-189. John Wiley & Sons Ltd, Chichester.
19. Gomis-Ruth F.X. Structure and mechanism of metallocarboxypeptidases. Crit. Rev. Biochem. Mol. Biol. 2008, 43(5):319-345.
20. Quiocho F.A., Lipscomb W.N. Carboxypeptidase A: a protein and an enzyme. Adv. Protein Chem. 1971, 25:1-78.
21. Hartsuck J.A., Lipscomb W.N. Carboxypeptidase A. The Enzymes 1971, Vol. 3:1-56. Academic Press, New York. 3rd edn.
22. Christianson D.W., Lipscomb W.N. Carboxypeptidase A. Acc. Chem. Res. 1989, 22:62-69.
23. Vallee B.L., Auld D.S. Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 1990, 29(24):5647-5659.
24. Auld D.S. Zinc enzymes. Encyclopedia of Inorganic Chemistry 2005, Vol. IX:5885-5927. John Wiley & Sons, Ltd., Chichester. 2nd ed.
25. Greenblatt H.M., Feinberg H., Tucker P.A., Shoham G. Carboxypeptidase A: native, zinc-removed and mercury-replaced forms. Acta Crystal. D Biol. Crystal. 1998, 54(Pt 3):289-305.
26. i value in the femtomolar range. Biochemistry 1991, 30(33):8165-8170.
27. Kim H., Lipscomb W.N. Comparison of the structures of three carboxypeptidase A-phosphonate complexes determined by X-ray crystallography. Biochemistry 1991, 30(33):8171-8180.
28. Mock W.L., Tsay J.T. Sulfoximine and sulfodiimine transition-state analogue inhibitors for carboxypeptidase A. J. Am. Chem. Soc. 1989, 111:4467-4472.
29. Cappalonga A.M., Alexander R.S., Christianson D.W. Structural comparison of sulfodiimine and sulfonamide inhibitors in their complexes with zinc enzymes. J. Biol. Chem. 1992, 267(27):19192-19197.
30. Kim D.H. Chemistry-based design of inhibitors for carboxypeptidase A. Curr. Top. Med. Chem. 2004, 4(12):1217-1226.
31. Mathur S., Park J.D., Kim D.H., Hartmann R.W. A method for screening enzyme inhibitors using size exclusion chromatography and ESI-LC-MS/MS. J. Biomol. Screen. 2005, 10(1):30-35.
32. Wang S.H., Wang S.F., Xuan W., Zeng Z.H., Jin J.Y., Ma J., Tian G.R. Nitro as a novel zinc-binding group in the inhibition of carboxypeptidase A. Bioorg. Med. Chem. 2008, 16(7):3596-3601.
33. Wang S.F., Tian G.R., Zhang W.Z., Jin J.Y. Characterization of alpha-nitromethyl ketone as a new zinc-binding group based on structural analysis of its complex with carboxypeptidase A. Bioorg. Med. Chem. Lett. 2009, 19(17):5009-5011.
34. Auld D.S., Galdes A., Geoghegan K.F., Holmquist B., Martinelli R.A., Vallee B.L. Cryospectrokinetic characterization of intermediates in biochemical reactions: carboxypeptidase A. Proc. Natl. Acad. Sci. USA 1984, 81(16):5041-5045.
35. Galdes A., Auld D.S., Vallee B.L. Cryokinetic studies of the intermediates in the mechanism of carboxypeptidase A. Biochemistry 1983, 22(8):1888-1893.
36. Geoghegan K.F., Galdes A., Martinelli R.A., Holmquist B., Auld D.S., Vallee B.L. Cryospectroscopy of intermediates in the mechanism of carboxypeptidase A. Biochemistry 1983, 22(9):2255-2262.
37. Galdes A., Auld D.S., Vallee B.L. Elucidation of the chemical nature of the steady-state intermediates in the mechanism of carboxypeptidase A. Biochemistry 1986, 25(3):646-651.
38. Auld D.S. Acyl group transfer-metalloproteinases. Enzyme Mechanisms 1987, 241-258. Royal Society of Chemistry, London. M.I. Page, A. Williams (Eds.).
39. Lipscomb W.N. Enzymatic activities of carboxypeptidase A's in solution and in crystals. Proc. Natl. Acad. Sci. USA 1973, 70(12):3797-3801.
40. Bauer R., Danielsen E., Hemmingsen L., Sorensen M.V., Ulstrup J., Friis E.P., Auld D.S., Bjerrum M.J. Structure and dynamics of the metal site of cadmium-substituted carboxypeptidase A in solution and crystalline states and under steady-state peptide hydrolysis. Biochemistry 1997, 36(38):11514-11524.
41. French T.C., Yu N.T., Auld D.S. Relaxation spectra of proteinases. Isomerizations of carboxypeptidase A (Cox) and (Anson). Biochemistry 1974, 13(14):2877-2882.
42. Geoghegan K.F., Holmquist B., Spilburg C.A., Vallee B.L. Spectral properties of cobalt carboxypeptidase A. Interaction of the metal atom with anions. Biochemistry 1983, 22(8):1847-1852.
43. Bicknell R., Schaffer A., Bertini I., Luchinat C., Vallee B.L., Auld D.S. Interaction of anions with the active site of carboxypeptidase A. Biochemistry 1988, 27(3):1050-1057.
44. Auld D.S., Bertini I., Donaire A., Messori L., Moratal J.M. pH-dependent properties of cobalt(II) carboxypeptidase A-inhibitor complexes. Biochemistry 1992, 31(15):3840-3846.
45. Zhang K., Auld D.S. Structure of binary and ternary complexes of zinc and cobalt carboxypeptidase A as determined by X-ray absorption fine structure. Biochemistry 1995, 34(50):16306-16312.
46. Larsen K.S., Auld D.S. Carboxypeptidase A: mechanism of zinc inhibition. Biochemistry 1989, 28(25):9620-9625.
47. Larsen K.S., Auld D.S. Characterization of an inhibitory metal binding site in carboxypeptidase A. Biochemistry 1991, 30(10):2613-2618.
48. Mock W.L., Wang L. Synergistic inhibition of carboxypeptidase A by zinc ion and imidazole. Biochem. Biophys. Res. Commun. 1999, 257(1):239-243.
49. Lee K.J., Joo K.C., Kim E.J., Lee M., Kim D.H. A new type of carboxypeptidase A inhibitors designed using an imidazole as a zinc coordinating ligand. Bioorg. Med. Chem. 1997, 5(10):1989-1998.
50. Auld D.S., Vallee B.L. Carboxypeptidase-A. Hydrolytic Enzymes 1987, 201-255. Elsevier, Amsterdam. H. Neuberger, K. Brocklehurst (Eds.).
51. Gomez-Ortiz M., Gomis-Ruth F.X., Huber R., Aviles F.X. Inhibition of carboxypeptidase A by excess zinc: analysis of the structural determinants by X-ray crystallography. FEBS Lett. 1997, 400(3):336-340.
52. Bukrinsky J.T., Bjerrum M.J., Kadziola A. Native carboxypeptidase A in a new crystal environment reveals a different conformation of the important tyrosine 248. Biochemistry 1998, 37(47):16555-16564.
53. Christianson D.W., Alexander R.S. Carboxylate-histidine-zinc interactions in protein structure and function. J. Am. Chem. Soc. 1989, 111:6412-6419.
54. Li X., Solomon B. Zinc-mediated thermal stabilization of carboxypeptidase A. Biomol. Eng. 2001, 18(4):179-183.
55. Nau H., Riordan J.F. Gas chromatography-mass spectrometry for probing the structure and mechanism of action of enzyme active sites. The role of Glu-270 in carboxypeptidase A. Biochemistry 1975, 14(24):5285-5294.
56. Kim D.H., Kim K.B. Design of a novel type of zinc-containing protease inhibitor. J. Amer. Chem. Soc. 1991, 113(8):3200-3202.
57. Tanaka Y., Grapsas I., Dakoji S., Cho J.Y., Mobashery S. Conscripting the active-site zinc ion in carboxypeptidase A in inactivation chemistry by a new type of irreversible enzyme inactivator. J. Amer. Chem. Soc. 1994, 1994(17):7475-7480.
58. Chai J.J., He C., Li M., Tang L., Luo M. Crystal structure of carboxypeptidase A complexed with an inactivator in two crystal forms. Protein Eng. 1998, 11(10):841-845.
59. Massova I., Martin P., de Mel S., Tanaka Y., Edwards B., Mobashery S. Crystallographic and computational insight on the mechanism of zinc-ion-dependent inactivation of carboxypeptidase A by 2-benzyl-3-iodopropanoate. J. Amer. Chem. Soc. 1996, 118:12479-12480.
60. Yun M., Park C., Kim S., Nam D., Kim S.C., Kim D.H. The X-ray crystallographic study of covalently modified carboxypeptidase A by 2-benzyl-3,4-epoxybutanoic acid, a pseudomechanism-based inactivator. J. Amer. Chem. Soc. 1992, 114:2281-2282.
61. Christianson D.W., Mangani S., Shoham G., Lipscomb W.N. Binding of -d-phenylalanine and -d-tyrosine to carboxypeptidase A. J. Biol. Chem. 1989, 264(22):12849-12853.
62. Lee S.S., Li Z.-H., Lee D.H., Kim D.H. (2R,3S)- and (2S,3R)-2-Benzyl-3,4-epoxybutanoic acid as highly efficient and fast acting pseudomechanism-based inactivators for carboxypeptidase A: design, asymmetric synthesis and inhibitory kinetics. J. Chem. Soc. Perkin Trans. 1995, 1:2877-2882.
63. Park J.D., Lee K.J., Kim D.H. A new inhibitor design strategy for carboxypeptidase A as exemplified by N-(2-chloroethyl)-N-methylphenylalanine. Bioorg. Med. Chem. 2001, 9(2):237-243.
64. Chung S.J., Chung S., Lee H.S., Kim E.J., Oh K.S., Choi H.S., Kim K.S., Kim Y.J., Hahn J.H., Kim D.H. Mechanistic insight into the inactivation of carboxypeptidase A by alpha-benzyl-2-oxo-1,3-oxazolidine-4-acetic acid, a novel type of irreversible inhibitor for carboxypeptidase A with no stereospecificity. J. Org. Chem. 2001, 66(19):6462-6471.
65. Fernandez D., Testero S., Vendrell J., Aviles F.X., Mobashery S. The X-ray structure of carboxypeptidase A inhibited by a thiirane mechanism-based inhibitor. Chem. Biol. Drug Des. 2010, 75(1):29-34.
66. Riordan J.F. Functional arginyl residues in carboxypeptidase A. Modification with butanedione. Biochemistry 1973, 12(20):3915-3923.
67. Phillips M.A., Fletterick R., Rutter W.J. Arginine 127 stabilizes the transition state in carboxypeptidase. J. Biol. Chem. 1990, 265(33):20692-20698.
68. Phillips M.A., Hedstrom L., Rutter W.J. Guanidine derivatives restore activity to carboxypeptidase lacking arginine-127. Protein Sci. 1992, 1(4):517-521.
69. Hilvert D., Gardell S.J., Rutter W.J., Kaiser E.T. Evidence against a crucial role for the phenolic hydroxyl of Tyr-248 in peptide and ester hydrolyses catalyzed by carboxypeptidase A: Comparative studies of the pH dependencies of the native and Phe-248-mutant forms. J. Am. Chem. Soc. 1986, 108:5298-5304.
70. Auld D.S., Larsen K., Vallee B.L. Active site residues of carboxypeptidase A. Zinc Enzymes 1986, Vol 1:133-154. Birkhauser, Boston, Vol. PBB.
71. Mock W.L., Tsay J.T. pK values for active site residues of carboxypeptidase A. J. Biol. Chem. 1988, 263(18):8635-8641.
72. Cho J.H., Kim D.H., Lee K.J., Choi K.Y. The role of Tyr248 probed by mutant bovine carboxypeptidase A: insight into the catalytic mechanism of carboxypeptidase A. Biochemistry 2001, 40(34):10197-10203.
73. Gardell S.J., Craik C.S., Hilvert D., Urdea M.S., Rutter W.J. Site-directed mutagenesis shows that tyrosine 248 of carboxypeptidase A does not play a crucial role in catalysis. Nature 1985, 317(6037):551-555.
74. Ghosh S.S., Dakoji S., Tanaka Y., Cho Y.J., Mobashery S. Properties of analogues of an intermediate in the process of mechanism-based inactivation of carboxypeptidase A. Bioorg. Med. Chem. 1996, 4(9):1487-1492.
75. Gardell S.J., Hilvert D., Barnett J., Kaiser E.T., Rutter W.J. Use of directed mutagenesis to probe the role of tyrosine 198 in the catalytic mechanism of carboxypeptidase A. J. Biol. Chem. 1987, 262(2):576-582.
76. Zhang K., Auld D.S. XAFS studies of carboxypeptidase A: detection of a structural alteration in the zinc coordination sphere coupled to the catalytically important alkaline pKa. Biochemistry 1993, 32(50):13844-13851.
77. Auld D.S. Zinc catalysis in metalloproteases. Structure and Bonding 1997, 89:29-50.
78. 2O of zinc enzymes. Proc. Natl. Acad. Sci. USA 1990, 87(1):220-224.
79. Neurath H., Bradshaw R.A., Petra P.H., Walsh K.A. Carboxypeptidase. Bovine carboxypeptidase A-activation, chemical structure and molecular heterogeneity. Philos. Trans. R. Soc. Lond. B Biol. Sci. 1970, 257(813):159-176.
80. Petra P.H. Bovine procarboxypeptidase and carboxypeptidase A. Methods Enzymol. 1970, 19:460-503.
81. Cox D.J., Bovard F.C., Bargetzi J.-P., Walsh K.A., Neurath H. Procedures for the isolation of crystalline bovine pancreatic carboxypeptidase A. II. Isolation of carboxypeptidase A, from procarboxypeptidase A. Biochemistry 1964, 3(1):44-47.
82. Allan B.J., Keller P.J., Neurath H. Procedures for the isolation of crystalline bovine pancreatic carboxypeptidase A. I. Isolation from acetone powders of pancreas glands. Biochemistry 1964, 3(1):40-43.
83. Petra P.H., Neurath H. Heterogeneity of bovine carboxypeptidase A. II. Chromatographic purification of carboxypeptidase A (Cox). Biochemistry 1969, 8(12):5029-5036.
84. Bicknell R., Schaeffer A., Auld D.S., Riordan J.F., Monnanni R., Bertini I. Protease susceptibility of zinc- and apo-carboxypeptidase A. Biochem. Biophys. Res. Commun. 1985, 133(2):787-793.
85. Bazzone T.J., Sokolovsky M., Cueni L.B., Vallee B.L. Single-step isolation and resolution of pancreatic carboxypeptidases A and B. Biochemistry 1979, 18(20):4362-4366.
86. Laethem R.M., Blumenkopf T.A., Cory M., Elwell L., Moxham C.P., Ray P.H., Walton L.M., Smith G.K. Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2. Arch. Biochem. Biophys. 1996, 332(1):8-18.
87. Darnis S., Juge N., Marino C., Aviles F.X., Puigserver A., Chaix J.C., Guo X.J. Cloning, sequencing and functional expression of a cDNA encoding porcine pancreatic preprocarboxypeptidase A1. Eur. J. Biochem. 1999, 259(3):719-725.
88. Riordan J.F. Metal-containing exopeptidases. Food Related Enzymes 1974, Vol. 136:220-240. American Chemical Society, Washington, D.C.
89. Wei S., Segura S., Vendrell J., Aviles F.X., Lanoue E., Day R., Feng Y., Fricker L.D. Identification and characterization of three members of the human metallocarboxypeptidase gene family. J. Biol. Chem. 2002, 277(17):14954-14964.
90. Clore G.M., Gronenborn A.M., Nilges M., Ryan C.A. Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. Biochemistry 1987, 26(24):8012-8023.
91. Rees D.C., Lipscomb W.N. Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 Å resolution. J. Mol. Biol. 1982, 160(3):475-498.
92. Reverter D., Fernandez-Catalan C., Baumgartner R., Pfander R., Huber R., Bode W., Vendrell J., Holak T.A., Aviles F.X. Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2. Nat. Struct. Biol. 2000, 7(4):322-328.
93. Arolas J.L., Lorenzo J., Rovira A., Castella J., Aviles F.X., Sommerhoff C.P. A carboxypeptidase inhibitor from the tick Rhipicephalus bursa: isolation, cDNA cloning, recombinant expression, and characterization. J. Biol. Chem. 2005, 280(5):3441-3448.
94. Willemse J.L., Heylen E., Nesheim M.E., Hendriks D.F. Carboxypeptidase U (TAFIa): a new drug target for fibrinolytic therapy?. J. Thromb. Haemost. 2009, 7(12):1962-1971.
95. Sanglas L., Arolas J.L., Valnickova Z., Aviles F.X., Enghild J.J., Gomis-Ruth F.X. Insights into the molecular inactivation mechanism of human activated thrombin-activatable fibrinolysis inhibitor. J. Thromb. Haemost. 2010, 8(5):1056-1065.
96. Valnickova Z., Sanglas L., Arolas J.L., Petersen S.V., Schar C., Otzen D., Aviles F.X., Gomis-Ruth F.X., Enghild J.J. Flexibility of the thrombin-activatable fibrinolysis inhibitor pro-domain enables productive binding of protein substrates. J. Biol. Chem. 2010, 285(49):38243-38250.
97. Arolas J.L., Popowicz G.M., Lorenzo J., Sommerhoff C.P., Huber R., Aviles F.X., Holak T.A. The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode. J. Mol. Biol. 2005, 350(3):489-498.
98. Crompton D.W. Ascaris and ascariasis. Adv. Parasitol. 2001, 48:285-375.
99. Sanglas L., Aviles F.X., Huber R., Gomis-Ruth F.X., Arolas J.L. Mammalian metallopeptidase inhibition at the defense barrier of Ascaris parasite. Proc. Natl. Acad. Sci. USA 2009, 106(6):1743-1747.
100. Normant E., Martres M.P., Schwartz J.C., Gros C. Purification, cDNA cloning, functional expression, and characterization of a 26-kDa endogenous mammalian carboxypeptidase inhibitor. Proc. Natl. Acad. Sci. USA 1995, 92(26):12225-12229.
101. Hatanaka Y., Uratani Y., Takiguchi-Hayashi K., Omori A., Sato K., Miyamoto M., Arimatsu Y. Intracortical regionality represented by specific transcription for a novel protein, latexin. Eur. J. Neurosci. 1994, 6(6):973-982.
102. Arimatsu Y. Latexin: a molecular marker for regional specification in the neocortex. Neurosci. Res. 1994, 20(2):131-135.
103. Uratani Y., Takiguchi-Hayashi K., Miyasaka N., Sato M., Jin M., Arimatsu Y. Latexin, a carboxypeptidase A inhibitor, is expressed in rat peritoneal mast cells and is associated with granular structures distinct from secretory granules and lysosomes. Biochem. J. 2000, 346(Pt. 3):817-826.
104. Itou Y., Suzuki S., Ishida K., Murakami M. Anabaenopeptins G and H, potent carboxypeptidase A inhibitors from the cyanobacterium Oscillatoria agardhii (NIES-595). Bioorg. Med. Chem. Lett. 1999, 9(9):1243-1246.
105. Murakami M., Suzuki S., Itou Y., Kodani S., Ishida K. New anabaenopeptins, potent carboxypeptidase-A inhibitors from the cyanobacterium Aphanizomenon flos-aquae. J. Nat. Prod. 2000, 63(9):1280-1282.
106. Kusano G., Takahira M., Shibano M., Kusano A., Okamoto Y., Tsujibo H., Numata A., Inamori Y. Studies on inhibitory activities of fukiic acid esters on germination, alpha-amylase and carboxypeptidase A. Biol. Pharm. Bull. 1998, 21(9):997-999.
107. Sakagami Y., Tsujibo H., Hirai Y., Yamada T., Numata A., Inamori Y. Inhibitory activities of 2-pyridinecarboxylic acid analogs on phytogrowth and enzymes. Biol. Pharm. Bull. 1999, 22(11):1234-1236.
108. Huennekens F.M. Tumor targeting: activation of prodrugs by enzyme-monoclonal antibody conjugates. Trends Biotechnol. 1994, 12(6):234-239.
109. Vitols K.S., Haag-Zeino B., Baer T., Montejano Y.D., Huennekens F.M. Methotrexate-alpha-phenylalanine: optimization of methotrexate prodrug for activation by carboxypeptidase A-monoclonal antibody conjugate. Cancer Res. 1995, 55(3):478-481.
110. Kuefner U., Lohrmann U., Montejano Y.D., Vitols K.S., Huennekens F.M. Carboxypeptidase-mediated release of methotrexate from methotrexate alpha-peptides. Biochemistry 1989, 28(5):2288-2297.
111. Perron M.J., Page M. Activation of methotrexate-phenylalanine by monoclonal antibody-carboxypeptidase A conjugate for the specific treatment of ovarian cancer in vitro. Br. J. Cancer 1996, 73(3):281-287.
112. Smith G.K., Banks S., Blumenkopf T.A., Cory M., Humphreys J., Laethem R.M., Miller J., Moxham C.P., Mullin R., Ray P.H., Walton L.M., Wolfe L.A. Toward antibody-directed enzyme prodrug therapy with the T268G mutant of human carboxypeptidase A1 and novel in vivo stable prodrugs of methotrexate. J. Biol. Chem. 1997, 272(25):15804-15816.
113. Wolfe L.A., Mullin R.J., Laethem R., Blumenkopf T.A., Cory M., Miller J.F., Keith B.R., Humphreys J., Smith G.K. Antibody-directed enzyme prodrug therapy with the T268G mutant of human carboxypeptidase A1: in vitro and in vivo studies with prodrugs of methotrexate and the thymidylate synthase inhibitors GW1031 and GW1843. Bioconjug. Chem. 1999, 10(1):38-48.
114. Wright J.E., Rosowsky A. Synthesis and enzymatic activation of N-[N(alpha)-(4-amino-4-deoxypteroyl)-N(delta)-hemiphthaloyl-l-ornithiny] -l-phenylalanine, a candidate for antibody-directed enzyme prodrug therapy (ADEPT). Bioorg. Med. Chem. 2002, 10(3):493-500.
115. Hamstra D.A., Page M., Maybaum J., Rehemtulla A. Expression of endogenously activated secreted or cell surface carboxypeptidase A sensitizes tumor cells to methotrexate-alpha-peptide prodrugs. Cancer Res. 2000, 60(3):657-665.
116. Lee J.W., Park J.H., Robinson J.R. Bioadhesive-based dosage forms: the next generation. J. Pharm. Sci. 2000, 89(7):850-866.
117. Luessen H.L., de Leeuw B.J., Langemeyer M.W., de Boer A.B., Verhoef J.C., Junginger H.E. Mucoadhesive polymers in peroral peptide drug delivery. VI. Carbomer and chitosan improve the intestinal absorption of the peptide drug buserelin in vivo. Pharm. Res. 1996, 13(11):1668-1672.
118. Pallares I., Fernandez D., Comellas-Bigler M., Fernandez-Recio J., Ventura S., Aviles F.X., Bode W., Vendrell J. Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid). Acta Crystallogr. D Biol. Crystallogr. 2008, D64(Pt. 7):784-891.
119. Auld D.S. Removal and replacement of metal ions in metallopeptidases. Methods Enzymol. 1995, 248:228-242.
120. Chong C.R., Auld D.S. Inhibition of carboxypeptidase A by d-penicillamine: Mechanism and implications for drug design. Biochemistry 2000, 39(25):7580-7588.
121. Chong C.R., Auld D.S. Catalysis of zinc transfer by d-penicillamine to secondary chelators. J. Med. Chem. 2007, 50(22):5524-5527.
122. Auld D.S. Zinc coordination sphere in biochemical zinc sites. BioMetals 2001, 14(3-4):271-313.
123. van Aalten D.M., Chong C.R., Joshua-Tor L. Crystal structure of carboxypeptidase A complexed with d-cysteine at 1.75 Å - inhibitor-induced conformational changes. Biochemistry 2000, 39(33):10082-10089.
124. Park J.D., Kim D.H. Cysteine derivatives as inhibitors for carboxypeptidase A: synthesis and structure-activity relationships. J. Med. Chem. 2002, 45(4):911-918.
125. Vallee B.L., Galdes A., Auld D.S., Riordan J.F. Carboxypeptidase A. Zinc Enzymes 1983, 26-75. John Wiley, New York. T.G. Spiro (Ed.).
126. Fernandez D., Pallares I., Vendrell J., Aviles F.X. Progress in metallocarboxypeptidases and their small molecular weight inhibitors. Biochimie 2010, 92(11):1484-1500.