Serrata) Alkaline Phosphatase

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1 Vol. 41, No. 5, April 1997 BIOCHEMISTRY and MOLECULAR BIOLOGY INTERNATIONAL Pages An Essential Tryptophan Residue of Green Crab (Syclla Serrata) Alkaline Phosphatase Wen-Zhu Zheng 1, Qing-Xi Chen l, Hong Zhao l, Zhe Zhang l, Wei Zhang 1 and Hai-Meng Zhou 2'* (1 Department of Biology, Xiamen University, Xiamen , 2 Department of Biological Science and Biotechnology, Tsinghua University, Beijing ~ China.) Received February 12, 1997 SUMMARY The tryptothan residues in green crab (scylla serrata) alkaline phosphatase (EC ) have been modified by N-bromosuccinimide (NBS). The modification of five tryptophan residues leads to complete loss of enzymatic activity. With the increase of NBS concentration, both the absorption at 278 nm and the fluorescence emission intensity at 335 nm of the modified enzyme decreased markedly indicating the modification of tryptophan residues. Quantitative treatment of the data (Tsou, Sci. Sinica 1962, 11, ) shows that among the tryptophan residues modified, one is essential for its catalytic activity. The presence of the substrate markedly protects the modification oftryptophan residues as well as the inactivation, suggesting that the essential tryptophan residue is situated at the active site of this enzyme~ Key words: Alkaline phosphatase; Essential residue; Chemical modification; Tryptophan. INTRODUCTION Alkaline phosphatase (ALP, EC 3,1.3.1) is a metalloenzyme which catalyzed the nonspecific hydrolysis of phosphatase monoesters [1]. The X-ray crystal structure of bacterial ALP has recently been reported to 2.0-A resolution in the presence of inorganic phosphate [2]. The active site is a pocket containing a tight cluster of two zinc ions (3.9-~ separation) and one magnesium ion (5 and 7A from the two zinc ions). ALP from green crab also is a metalloenzyme containing zinc and magnesium ions, and the structure of its Abbreviations: ALP, alkaline phosphatase; PNPP, p-nitrophenyl phosphate; NBS, N-bromosueinimide. * To whom correspondence should be addressed /97/ /0 Copyright by Academic Press Australia. 951 All rights of reproduction in any form reserved.

2 active site probably is similar to that of bacterial ALP. It is well known that the arginine residue is essential residue for activity of green crab ALP [3]. Kinetics of inhibition of green crab alkaline phosphatase by NBS have been reported [4]. In the preset investigation, we have now shown that the tryptophan residues are modified by NBS, and quantitative assessment (Tsou, 1962) of the tad indicates that one of them is essential for the catalytic activity of this enzyme. MATERIALS AND METHODS The Alkaline phoshatase was prepared from green crab (Scylla serrata)viscera first according to the method of Yan and Chen [5] to the step of ammonium sulfate fractionation; the crude preparation was further chromatographed by ionexchange with DEAE-cellulose (DE-32), then by gel filtration through Sephadex G-150 followed by DEAE-Sephadex A-50. The final preparation was homogeneous on polyacrylamide gel isoelectric focusing electrophoresis and HPLC chromatography. The specific activity of the purified enzyme was 3320u/mg. p-nitrophenylphosphate (PNPP)was from E. Merck; N- bromosuccinimide (NBS) was a Sigma product; DEAE-ceUulose (DE-32)was from Whatman; Sephadex G-150 and DEAE-Sephadex A-50 were Pharmacia products. All other reagents were local products of analytical grade. Enzyme concentration was determined as described by Lowry [6]. Enzyme activity was determined at 30~ by following the increasing absorbance 405 nm accompanying the hydrolysis of the substrate (p-nitrophenylphosphate)with the molar absorption coefficient of 1.73x104M-Icm l. The reaction system contained p-nitrophenylphosphate, 2mM; MgC12, 2mM; and Na2CO~fNaHCO3 buffer, 0.05 M (phi0.0). Modification of the enzyme was carried out in 0.1M Tris-HC1 buffer (ph 7.5) with different amounts of NBS. After 5 min, 5 gl of reaction mixture was used for assay activity as described by Chen and Yan (1986). The kinetics of inhibition of green crab ALP by NBS was analyzed as described before [7]. The tryptophan residues of the enzyme was determined by the DAB method [81. A Shimadzu UV-240 spectrophotometer and a Hitachi F-4010 spectrofluorometer were used for absorbance and fluorescence measurements respectively. All measurements were carried out at 25 ~ C. 952

3 RESULTS The effect o[ modification of the SH groups on the enzymatic activity N-bromosuccinimide can react with indole group of tryptophan and SH group of cysteine for a number of proteins. Therefore, we have to know that the effect of modification of the SH groups on the activity of the enzyme before modification of tryptophan residues. Treatment of native green cab ALP with PCMB at a 500-fold molar excess not led to inactivation of the enzyme, indicating that the SH groups of cysteine residues of the enzyme are non-essential for its catalytic activity. Fig. 1 shows the effect of modification of the SH groups on the enzymatic activity. Modification of the tryptophan residues The reactive tryptophan residues of the enzyme was determined using DAB method [8]. The obtained results (Table 1) show that each molecule of the enzyme contains five reactive tryptophan residues. The enzyme was treated with different amounts of NBS in 0.1 M Tris-HC1 buffer (ph 7.5). After incubation for 5 min, 5 gl of reaction mixture was used for activity assay. Fig. 1 shews that with increasing the concentration of NBS, the activity of the enzyme decreased to reach the complete inactivation when the concentration of NBS was 2 mm It has been reported that some proteins with tryptophan residues modified by NBS has a decrease of absorption at 278 nm [9,10]. Fig. 2 shows that the absorbance spectra of the modified ALP treated with different concentrations of NBS. It can be seen that modification of the tryptophan residues results in a decrease in absorption at 278 nm. The intrinsic fluorescence emission spectra of the native and the modified enzyme are shown in Fig3. As an excitation wavelength of 282 nm was used, the decrease in fluorescence shows essentially the modification of the tryptophane residues. With the increase of the concentration of NBS, the fluorescence emission intensity at 335 nm 953

4 BIOCHEMISTRY and MOLECULAR BIOLOGY INTERNATIONAL 100~ w 8O 60 < Concentration of inhibition (mmol/l) Fig. 1. Inactivation of green crab alkaline phosphatase by PCMB and NBS Alkaline phosphatase, in 0.1 M Tris-HC1 buffer (ph 7.5), was mixed with PCMB ( 9 ) or NBS ( o ) of different concentrations in the same buffer to a final concentration of 14/,tM. Samples were taken after incubation for 5 rain at 25~ for measurement of activity remaining. Table 1. Determination of numbers of tryptophan residues in the enzyme molecule Enzyme amount (~tm) 1.40 x x x 10.3 Tryptophan residue 0xM) 6.80 x x lff x 10-3 Trp tool. / ALP mol decreased in magnitude to reach minimal value at 2 mm NBS. For the emission spectra of the modified ALP with different modified extents, no marked red-shift was obtained. It suggests that the tryptophan residues relatively close to the surface of the molecule have been modified. No gross conformational change has occurred. Quantitative assessment of the number of the essesntial tryptophan residues The above results show that the enzyme showed decreased activity depending on the amount of tryptophan residues modified. Fig. 4 shows the relationship between the 954

5 ,~ 0.2 < Wavelength (nm) Fig. 2. Absorption spectra of NBS-modified alkaline phosphatase. Experimental conditions were as for Fig. 1. The concentration of NBS for curves 1-4 was o, 1.0, 1.5 and 2.0 mm, respectively. i / Wavelength (nm) Fig.3. Fluorescence emission spectra of green crab alkaline phosphatase modified by NBS. Experimental conditions were as for Fig. 1. The concentration of NBS for curves 1-5 was 0, 0.5, 1.0, 1.5 and 2.0 mm, respectively. 955

6 1.0( i 0.8 I I I X Fig. 4. Fraction of ALP activity remaining (a) plotted against the fraction of residual Trp residues. For details see text. fractional activity remaining (a) and the fractional residue remaining (x) of the enzyme as a Tsou plot [4]. It can be seen from Fig. 4 that two fast reaction residues have not effected on the enzymatic activity and that among the three slow reaction tryptophan residues modified only one is essential for the activity of the enzyme. Kinetics of modification oft he enzyme by NBS The kinetic method &the substrate reaction previously described by Tsou (1988) was used for the study of the inactivation kinetics of green crab alkaline phosphatase. 5 p,1 of 15 ~M ALP was added to 1.0 ml of reaction mixture containing 1.33 mm substrate in 0.05 M Na2CO3/NaHCO3 buffer (ph 10.0) containing different concentrations of NBS. The time course of the hydrolysis of the substrate in the presence of different NBS concentrations is shown in Fig. 5a. As described before [10], Plots of ln([p]~,lc - [P]t) against t give a series of straight lines at different concentrations of NBS with slopes of-(a[y] + B), as shown in Fig. 5b. (A[Y] + B) is the apparent rate constants of inactivation, i.e. the first order rate constants kl. The values of kl at the different concentrations of NBS can be obtained from 956

7 BIOCHEMISTRY and MOLECULAR BIOLOGY INTERNATIONAL ~" '180 Time (sec) o., ~ Fig. 5.,,, Time (min) lg INBSI (~ mot/l) Kinetics of substrate reaction in the presence of different concentrations of NBS. Conditions were 0.05 M Na2CO3/NaHCOs buffer (ph 10.0), 2 mm MgC12, and 1.33 mm PNPP. Final concentration of the enzyme was um. (a) Time courses of substrate reaction. Concentration of NBS for curves 0-5 was 0, 40, 60, 70, 80 and 200 ~M, respectively. (b) Semilogarithmic plots of ln([p]~,lc - [Pit) against time to determine the apparent first order rate constants (kt). ascertain the number of essential Trp residue of the enzyme. (c) Secondary plot of lg kx against lg [NBS] to the slopes of the straight lines. The results show that with the increase of NBS concentration, the value of k~ increased. The relationship between kl and the inhibitor concentration [I] can be written [ 11 ]: kl = k2[i]" or lg kl = lg k2 + n lg [I] where k~ and k2 are the first and second order rate constants of inactivation, respectively. [I] is the concentration of the inhibitor NBS The n is the numbers of essential residues modified. Plot oflg kl against lg [I] gives a straight line, as shown in Fig. 5c, where the slope of the straight line gives the value of n (n = 0.98). The obtained result shows that among the five tryptophan residues modified only one is essential for the activity of the 957

8 0.6..~ // [NBS] (i a mol/l) Fig. 6. A plot ofk~ against the concentration of NBS to determine the second order rate constant k2 of inactivation of the enzyme by NBS. enzyme. A plot of k~ against [NBS] gives a straight line which passes through on original point of the coordinate, as shown in Fig 6 where the slope of the straight line gives the second order rate constant k2 (6.25 x 103 min~mz). DISCUSSION It is known that NBS can react with the indole group of tryptophan and SH group of cysteine for a number of proteins. Our results have shown the modification of SH groups not effects on catalytic activity of the enzyme. Therefore, the results presented in the above sections show clearly that the modification of tryptophan residues of green crab alkaline phosphatase by high concentrations of NBS leads to the complete inactivation of this enzyme. The linearity of the plot shows that among the five tryptophan residues modified only one is essential for the activity of the enzyme. The analysis for inactivation rate and Try residue modification rate also shows that among all modified residues only one is essential Trp residue, The absorption decrease at 278 nm and the fluorescence intensity quenching at 335 nm indicate the loss of Trp residues of the enzyme. The results from the kinetic analysis show a marked protective effect of the substrate on the inactivation reaction of the enzyme by NBS. The above results suggest that the presence of tryptophan residue at or near the active site, and this residue is essential for the activity of the enzyme. 958

9 ACKNOWLEDGMENTS The present investigation was supported in par by Grant of the China Natural Science Foundation to Q.X.Chen, and Grant of the China Natural Science Foundation to H.MZhou REFERENCES 1. McComb,R.B., Bower, G.N and Posen, S. (1979)Alkaline Phosphatase, Plenum Press, New York. 2. Kim,EE and Wyckoff, H.W. (1991) J. Mol. Biol. 218, Xie,W.Z., Wang,H.R., Chen, Q.X. and Zhou,H.M. (1996)Biochem. Mol. Biol. Int. 40(5), Tsou,C.L. (1962) Sci. Sinica 11, Yan, SX. and Chen,Q.X. (1985) J. Xiamen Univ. 24(3), (in Chinese). 6. Lowry,OH. (1951) J. Biol. Chem. 193, Chen, Q.X., Zhang,W., Zheng,W.Z., Zhao,H.,Yan, S.X., Wang,HR. and Zhou,H.M. (1996) J. Protein Chem. 15(4), Cai,W.C. (1982) Chemical Analysis Methods of Biological Materials, Chinese Science press, Beijing. 9. Freisheim,J.H. and Huennekens,F.M. (1969) Biochemistry 8, Chen, Q.X. and Yan, S.X. (1986) J.Xiamen Univ. 25(5), (in Chinese). 11. Hollenberg,P.F. (1971)J. Biol. Chem. 246,

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