Crystalline l-Aspartate β-Decarboxylase of Pseudomonas dacunhae

作者: Toshio Kakimoto , Jyoji Kato , Takeji Shibatani , Noriyuki Nishimura , Ichiro Chibata

DOI: 10.1016/S0021-9258(18)63005-4

关键词:

摘要: l -Aspartate β-decarboxylase ( -aspartate 4-carboxy-lyase) of Pseudomonas dacunhae has a molecular weight about 800,000. On treatment with 1 m guanidine the enzyme dissociates into subunits intermediate size (mol wt = 400,000, s 5.6 S). Removal by dialysis results in reassociation to native enzyme. Irreversible dissociation an ultimate subunit 100,000, s20,w0 6.9 S) occurs on 5 guanidine. presence 0.1 mercaptoethanol, this smaller polypeptide chains 50,000, 4.2 Aspartate contains 32 sulfhydryl groups per 800,000 g protein as determined titration p-chloromercuribenzoate The number half-cystine residues is 48 amino acid analysis. Also 8 disulfide molecule were found. Phenylthiocarbamylation apodecarboxylase urea gives 0.87 (corrected) mole serine phenylthiohydantoin hydrolysis, and hydrazinolysis 0.73 lysine 50,000 Digestion carboxypeptidase B 2 releases 0.98 evidence from these analyses suggests that consists 100,000 each composed two apparently identical 50,000) covalently linked through single linkage. Amino analysis also presented.

参考文章(50)
L. V. Crawford, Studies on the aspartic decarboxylase of Nocardia globerula. Biochemical Journal. ,vol. 68, pp. 221- 225 ,(1958) , 10.1042/BJ0680221
D.A. Wilson, I.P. Crawford, Purification and Properties of the B Component of Escherichia coli Tryptophan Synthetase Journal of Biological Chemistry. ,vol. 240, pp. 4801- 4808 ,(1965) , 10.1016/S0021-9258(18)97026-2
Abraham Novogrodsky, Jonathan S. Nishimura, Alton Meister, Transamination and β-Decarboxylation of Aspartate Catalyzed by the Same Pyridoxal Phosphate-Enzyme Journal of Biological Chemistry. ,vol. 238, pp. 1903- ,(1963) , 10.1016/S0021-9258(18)81155-3
W. Terry Jenkins, David A. Yphantis, Irwin W. Sizer, Glutamic aspartic transaminase. I. Assay, purification, and general properties. Journal of Biological Chemistry. ,vol. 234, pp. 51- 57 ,(1959) , 10.1016/S0021-9258(18)70333-5
Abraham Novogrodsky, Alton Meister, Control of Aspartate β-Decarboxylase Activity by Transamination Journal of Biological Chemistry. ,vol. 239, pp. 879- 888 ,(1964) , 10.1016/S0021-9258(18)51672-0
Gerald R. Seaman, Amino acid decarboxylases in a pseudomonad. Journal of Bacteriology. ,vol. 80, pp. 830- 836 ,(1960) , 10.1128/JB.80.6.830-836.1960
E A Boeker, E E Snell, Arginine Decarboxylase from Escherichia coli II. DISSOCIATION AND REASSOCIATION OF SUBUNITS Journal of Biological Chemistry. ,vol. 243, pp. 1678- 1684 ,(1968) , 10.1016/S0021-9258(18)93499-X
Stanford Moore, On the determination of cystine as cysteic acid. Journal of Biological Chemistry. ,vol. 238, pp. 235- 237 ,(1963) , 10.1016/S0021-9258(19)83985-6
O. Vesterberg, T. Wadström, K. Vesterberg, H. Svensson, B. Malmgren, Studies on extracellular proteins from Staphylococcus aureus Biochimica et Biophysica Acta (BBA) - Protein Structure. ,vol. 133, pp. 435- 445 ,(1967) , 10.1016/0005-2795(67)90547-8
Kazuo Kawahara, Charles Tanford, Viscosity and density of aqueous solutions of urea and guanidine hydrochloride. Journal of Biological Chemistry. ,vol. 241, pp. 3228- 3232 ,(1966) , 10.1016/S0021-9258(18)96519-1