The enzymatic activity of phosphoglycerate mutase from gram-positive endospore-forming bacteria requires Mn2+ and is pH sensitive

被引:45
作者
Chander, M [1 ]
Setlow, B [1 ]
Setlow, P [1 ]
机构
[1] Univ Connecticut, Ctr Hlth, Dept Biochem, Farmington, CT 06030 USA
关键词
Bacillus; Clostridium; Mn2+; phosphoglycerate mutase; sporulation;
D O I
10.1139/cjm-44-8-759
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The enzymatic activity of phosphoglycerate mutase (Pgm) from three gram-positive endospore-forming bacteria (Bacillus subtilis, Clostridium perfringens, and Sporosarcina ureae) requires Mn2+ and is very sensitive to pH; at low concentrations of Mn2+, a pH change from 8 to 6 resulted in greater than 30- to 200-fold decreases in the activity of these Pgms. However, Pgm deactivation at pH 6 was reversed by shifting the enzyme to pH 7 or 8. Free Mn2+ was not directly involved in Pgm catalysis, although enzyme-bound Mn2+ may be involved. The rate of catalysis by Mn2+-containing Pgm was also slightly pH dependent, although the K-m for 3-phosphoglyceric acid appeared to be the same at pH 6, 7, and 8. These findings suggest that Mn2+ binds to catalytically inactive Pgm and converts it to a catalytically competent form, and further, that pH influences the efficiency with which the enzyme binds Mn2+. The extreme pH sensitivity of the Mn2+-dependent Pgms supports a model in which this enzyme is inhibited during sporulation by acidification of the forespore, thus allowing accumulation of the spore's large depot of 3-phosphoglyceric acid. The activity of Pgm from two closely related gram-positive bacteria that do not form spores (Planococcus citreus and Staphylococcus saprophyticus) also requires Mn2+ and is pH sensitive. In contrast, the Pgm activities from two more distantly related non-endospore-forming gram-positive bacteria (Micrococcus luteus and Streptomyces coelicolor) are neither dependent on metal ions nor particularly sensitive to pH.
引用
收藏
页码:759 / 767
页数:9
相关论文
共 27 条
[1]  
ASH DE, 1982, J BIOL CHEM, V257, P9261
[2]  
BUCHER T, 1964, HOPPESEYLER THIERF A, V6, P292
[3]   VANADATE INHIBITS 2,3-BISPHOSPHOGLYCERATE DEPENDENT PHOSPHOGLYCERATE MUTASES BUT DOES NOT AFFECT THE 2,3-BISPHOSPHOGLYCERATE INDEPENDENT PHOSPHOGLYCERATE MUTASES [J].
CARRERAS, J ;
BARTRONS, R ;
GRISOLIA, S .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1980, 96 (03) :1267-1273
[4]  
FOTHERGILLGILMO.LA, 1989, ADV ENZYMOL RAMB, V62, P227
[5]   HYDROGEN ION BUFFERS FOR BIOLOGICAL RESEARCH [J].
GOOD, NE ;
WINGET, GD ;
WINTER, W ;
CONNOLLY, TN ;
IZAWA, S ;
SINGH, RMM .
BIOCHEMISTRY, 1966, 5 (02) :467-&
[6]   BIOCHEMICAL PROPERTIES OF CLOSTRIDIUM-BIFERMENTANS SPORES [J].
HAUSENBAUER, JM ;
WAITES, WM ;
SETLOW, P .
JOURNAL OF BACTERIOLOGY, 1977, 129 (02) :1148-1150
[7]   Structure of a unique binuclear manganese cluster in arginase [J].
Kanyo, ZF ;
Scolnick, LR ;
Ash, DE ;
Christianson, DW .
NATURE, 1996, 383 (6600) :554-557
[8]   PH-SENSITIVE CONTROL OF ARGINASE BY MN(II) IONS AT SUBMICROMOLAR CONCENTRATIONS [J].
KUHN, NJ ;
TALBOT, J ;
WARD, S .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1991, 286 (01) :217-221
[9]   COOPERATIVE MANGANESE(II) ACTIVATION OF 3-PHOSPHOGLYCERATE MUTASE OF BACILLUS-MEGATERIUM - A BIOLOGICAL PH-SENSING MECHANISM IN BACTERIAL SPORE FORMATION AND GERMINATION [J].
KUHN, NJ ;
SETLOW, B ;
SETLOW, P ;
CAMMACK, R ;
WILLIAMS, R .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1995, 320 (01) :35-42
[10]   MANGANESE(II) ACTIVATION OF 3-PHOSPHOGLYCERATE MUTASE OF BACILLUS-MEGATERIUM - PH-SENSITIVE INTERCONVERSION OF ACTIVE AND INACTIVE FORMS [J].
KUHN, NJ ;
SETLOW, B ;
SETLOW, P .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1993, 306 (02) :342-349