Structure-based approach to alter the substrate specificity of Bacillus subtilis aminopeptidase

Prion

Volumn 7, Issue 4, 2013, Pages 328-334

  Gao, Xinxing ^a   Cui, Wenjing ^a   Ding, Ning ^a   Liu, Zhongmei ^a   Tian, Yaping ^a   Zhou, Zhemin ^a  

^a JIANGNAN UNIVERSITY   (China)

Author keywords

Aminopeptidase; Bacillus subtilis; Protein hydrolysis; Saturation mutagenesis; Substrate specificity

Indexed keywords

AMINOPEPTIDASE; ARGININE; HYDROLASE; LEUCINE; LYSINE; TRANSCRIPTION FACTOR PAX5;

ARTICLE; BACILLUS SUBTILIS; BACTERIUM CULTURE; CATALYSIS; CONTROLLED STUDY; ENZYME SPECIFICITY; ENZYME STRUCTURE; GENE MUTATION; MUTAGENESIS; NONHUMAN; PROTEIN CLEAVAGE; PROTEIN HYDROLYSIS;

AMINOPEPTIDASE; BACILLUS SUBTILIS; PROTEIN HYDROLYSIS; SATURATION MUTAGENESIS; SUBSTRATE SPECIFICITY;

AMINO ACID SUBSTITUTION; AMINOPEPTIDASES; BACILLUS SUBTILIS; HYDROLYSIS; MUTATION, MISSENSE; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 84886880621     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.25147     Document Type: Article

References (30)

1. Gonzales T, Robert-Baudouy J. Bacterial aminopeptidases: properties and functions. FEMS Microbiol Rev 1996; 18:319-44; PMID:8703509; http://dx.doi.org/10.1111/j.1574-6976.1996.tb00247.x
2. Kilcawley KN, Wilkinson MG, Fox PF. Determination of key enzyme activities in commercial peptidase and lipase preparations from microbial or animal sources. Enzyme Microb Technol 2002; 31:310-20; http://dx.doi.org/10. 1016/S0141-0229(02)00136-9
3. Taylor A. Aminopeptidases: towards a mechanism of action. Trends Biochem Sci 1993; 18:167-71; PMID:8328016
4. Pulido-Cejudo G, Conway B, Proulx P, Brown R, Izaguirre CA. Bestatin-mediated inhibition of leucine aminopeptidase may hinder HIV infection. Antiviral Res 1997; 36:167-77; PMID:9477117; http://dx.doi.org/10.1016/S0166- 3542(97)00052-1
5. Holz RC, Bzymek KP, Swierczek SI. Co-catalytic metallopeptidases as pharmaceutical targets. Curr Opin Chem Biol 2003; 7:197-206; PMID:12714052; http://dx.doi.org/10.1016/S1367-5931(03)00033-4
6. Bauvois B. Transmembrane proteases in cell growth and invasion: new contributors to angiogenesis? Oncogene
7. Guo Y, Pan D, Tanokura M. Optimisation of hydrolysis conditions for the production of the angiotensin-I converting enzyme (ACE) inhibitory peptides from whey protein using response surface methodology. Food Chem 2009; 114:328-33; http://dx.doi.org/10.1016/j. foodchem.2008.09.041
8. Su G, Ren J, Yang B, Cui C, Zhao M. Comparison of hydrolysis characteristics on defatted peanut meal proteins between a protease extract from Aspergillus oryzae and commercial proteases. Food Chem 2011; 126:1306-11; http://dx.doi.org/10.1016/j.foodchem. 2010.11.083
9. Wang F, Ning Z, Lan D, Liu Y, Yang B, Wang Y. Biochemical properties of recombinant leucine aminopeptidase II from Bacillus stearothermophilus and potential applications in the hydrolysis of Chinese anchovy (Engraulis japonicus) proteins. J Agric Food Chem 2012; 60:165-72; PMID:22148180; http://dx.doi.org/10.1021/jf204002e
10. Zhu X, Barman A, Ozbil M, Zhang T, Li S, Prabhakar R. Mechanism of peptide hydrolysis by co-catalytic metal centers containing leucine aminopeptidase enzyme: a DFT approach. J Biol Inorg Chem 2012; 17:209-22; PMID:21918843; http://dx.doi.org/10.1007/s00775-011-0843-2
11. Gao X, Cui W, Tian Y, Zhou Z. Over-expression, secretion, biochemical characterisation, and structure analysis of Bacillus subtilis aminopeptidase. J Sci Food Agric 2013; (accepted); PMID:23426795; http://dx.doi.org/10.1002/jsfa. 6105
12. Chen G, Edwards T, D'souza VM, Holz RC. Mechanistic studies on the aminopeptidase from Aeromonas proteolytica: a two-metal ion mechanism for peptide hydrolysis. Biochemistry 1997; 36:4278-86; PMID:9100023; http://dx.doi.org/10.1021/bi9618676
13. Fundoiano-Hershcovitz Y, Rabinovitch L, Langut Y, Reiland V, Shoham G, Shoham Y. Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus. FEBS Lett 2004; 571:192-6; PMID:15280041; http://dx.doi.org/10.1016/j.febslet. 2004.07.001
14. Gilboa R, Spungin-Bialik A, Wohlfahrt G, Schomburg D, Blumberg S, Shoham G. Interactions of Streptomyces griseus aminopeptidase with amino acid reaction products and their implications toward a catalytic mechanism. Proteins 2001; 44:490-504; PMID:11484227; http://dx.doi.org/10.1002/prot.1115
15. Hershcovitz YF, Gilboa R, Reiland V, Shoham G, Shoham Y. Catalytic mechanism of SGAP, a doublezinc aminopeptidase from Streptomyces griseus. FEBS J 2007; 274:3864-76; PMID:17608735; http://dx.doi.org/10.1111/j.1742-4658.2007. 05912.x
16. Munih P, Moulin A, Stamper CC, Bennett B, Ringe D, Petsko GA, et al. X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica. J Inorg Biochem 2007; 101:1099-107; PMID:17574677; http://dx.doi.org/10.1016/j.jinorgbio.2007.03.010
17. Chen SL, Marino T, Fang WH, Russo N, Himo F. Peptide hydrolysis by the binuclear zinc enzyme aminopeptidase from Aeromonas proteolytica: a density functional theory study. J Phys Chem B 2008; 112:2494-500; PMID:18247603; http://dx.doi.org/10.1021/jp710035j
18. Luo X, Hofmann K. The protease-associated domain: a homology domain associated with multiple classes of proteases. Trends Biochem Sci 2001; 26:147-8; PMID:11246007; http://dx.doi.org/10.1016/S0968-0004(00)01768-0
19. Mahon P, Bateman A. The PA domain: a protease-associated domain. Protein Sci 2000; 9:1930-4; PMID:11106166; http://dx.doi.org/10.1110/ps.9.10.1930
20. O'Farrell HC, Musayev FN, Scarsdale JN, Rife JP. Control of substrate specificity by a single active site residue of the KsgA methyltransferase. Biochemistry 2012; 51:466-74; PMID:22142337; http://dx.doi.org/10.1021/bi201539j
21. Arima J, Uesugi Y, Iwabuchi M, Hatanaka T. Alteration of leucine aminopeptidase from Streptomyces septatus TH-2 to phenylalanine aminopeptidase by site-directed mutagenesis. Appl Environ Microbiol 2005; 71:7229-35; PMID:16269763; http://dx.doi.org/10.1128/AEM.71.11.7229-7235.2005
22. Arima J, Uesugi Y, Iwabuchi M, Hatanaka T. Change in substrate preference of Streptomyces aminopeptidase through modification of the environment around the substrate binding site. Appl Environ Microbiol 2006; 72:7962-7; PMID:17028223; http://dx.doi.org/10.1128/AEM.01460-06
23. Arima J, Uesugi Y, Uraji M, Iwabuchi M, Hatanaka T. The role of Glu196 in the environment around the substrate binding site of leucine aminopeptidase from Streptomyces griseus. FEBS Lett 2006; 580:912-7; PMID:16427629; http://dx.doi.org/10.1016/j.febslet. 2006.01.014
24. Monné M, Miniero DV, Daddabbo L, Robinson AJ, Kunji ERS, Palmieri F. Substrate specificity of the two mitochondrial ornithine carriers can be swapped by single mutation in substrate binding site. J Biol Chem 2012; 287:7925-34; PMID:22262851; http://dx.doi.org/10.1074/jbc.M111.324855
25. Zyprian E, Matzura H. Characterization of signals promoting gene expression on the Staphylococcus aureus plasmid pUB110 and development of a gram-positive expression vector system. DNA 1986; 5:219-25; PMID:3013549; http://dx.doi.org/10.1089/dna.1986.5.219
26. Wu XC, Lee W, Tran L, Wong SL. Engineering a Bacillus subtilis expression-secretion system with a strain deficient in six extracellular proteases. J Bacteriol 1991; 173:4952-8; PMID:1907264
27. Spizizen J. Transformation of Biochemically Deficient Strains of Bacillus Subtilis by Deoxyribonucleate. Proc Natl Acad Sci U S A 1958; 44:1072-8; PMID:16590310; http://dx.doi.org/10.1073/pnas.44.10.1072
28. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72:248-54; PMID:942051; http://dx.doi.org/10.1016/0003- 2697(76)90527-3
29. Nilsang S, Lertsiri S, Suphantharika M, Assavanig A. Optimization of enzymatic hydrolysis of fish soluble concentrate by commercial proteases. J Food Eng 2005; 70:571-8; http://dx.doi.org/10.1016/j. jfoodeng.2004.10.011
30. Miller J, Young CT. Protein nutritional quality of Florunner peanut meal as measured by rat bioassay. J Agric Food Chem 1977; 25:653-7; PMID:858861; http://dx.doi.org/10.1021/jf60211a051