Dissociation and catalytic activity of phosphate-repressible alkaline phosphatase from Neurospora crassa

1989 ◽  
Vol 28 (12) ◽  
pp. 3281-3284 ◽  
Author(s):  
M.S. Palma ◽  
S.W. Han ◽  
A. Rossi
1995 ◽  
Vol 8 (9) ◽  
pp. 865-871 ◽  
Author(s):  
Chris G. Dealwis ◽  
Liqing Chen ◽  
Catherine Brennan ◽  
Wlodek Mandecki ◽  
Cele Abad-Zapatero

1966 ◽  
Vol 241 (7) ◽  
pp. 1468-1472 ◽  
Author(s):  
Joseph F. Nyc ◽  
Robert J. Kadner ◽  
Barbara J. Crocken

Isozymes ◽  
1975 ◽  
pp. 343-365 ◽  
Author(s):  
RODY P. COX ◽  
NIMAI K. GHOSH ◽  
KIRSTAN BAZZELL ◽  
MARTIN J. GRIFFIN

1989 ◽  
Vol 35 (9) ◽  
pp. 830-835 ◽  
Author(s):  
E. Nahas

Repressible acid, repressible alkaline, and constitutive alkaline phosphatases were studied with respect to their control and localization in conidia of Neurospora crassa. In contrast to constitutive alkaline phosphatase, the production and secretion of repressible phosphatases is regulated by phosphate level and pH of the culture medium. Phosphatase activity increased with conidial germination and was detectable partially in the growth medium after 5 h incubation. These enzymes were found to be located in different cell compartments. Part of the whole cell enzyme activity involved a soluble exoconidial fraction, and another part, a cell-bound enzyme that remained after successive washes. The cell-bound enzyme was sensitive to treatment with dilute acid and was thought to be located in the mural space. A third part of the enzyme activity was judged to be intracellular, as shown by treatments with surface-active agents and heat, which disrupted the conidia or destroyed the conidial permeability barriers. On the basis of these criteria, the constitutive alkaline phosphatase was considered to be more cryptic than the repressible phosphatases. The alkaline phosphatases were also active during heat treatment, suggesting they may be involved in the mechanism of secretion.Key words: Neurospora crassa, repressible acid phosphatase, repressible alkaline phosphatase, constitutive alkaline phosphatase, conidia.


2000 ◽  
Vol 294 (1-2) ◽  
pp. 57-66
Author(s):  
S.J Iqbal ◽  
P Whitaker ◽  
S Holland ◽  
W Madira ◽  
T Davies

1996 ◽  
Vol 41 (1) ◽  
pp. 71-75 ◽  
Author(s):  
JoséC. Say ◽  
Rosa P.M. Furriel ◽  
Pietro Ciancaglini ◽  
João A. Jorge ◽  
Maria Lourdes ◽  
...  

1995 ◽  
Vol 11 (5) ◽  
pp. 505-507 ◽  
Author(s):  
M. Pereira ◽  
H. Pereira ◽  
G. Thedei ◽  
A. Rossi ◽  
N. M. Martinez-Rossi

Genetics ◽  
1973 ◽  
Vol 75 (1) ◽  
pp. 61-73
Author(s):  
John F Lehman ◽  
Mary K Gleason ◽  
Sandra K Ahlgren ◽  
Robert L Metzenberg

ABSTRACT A mutant of Neurospora crassa, called UW-6, differs from wild type in being partially constitutive for synthesis of a species of alkaline phosphatase, and also for a species of phosphate permease that has a high affinity for phosphate at high pH. UW-6 is possibly allelic with a mutant called nuc-2 that was previously isolated by Ishikawa. nuc-2 has the converse phenotype, in that it cannot be derepressed for either of these two activities. UW-6 is co-dominant with its wild-type allele in heterokaryons and in partial diploids. An unlinked mutant, nuc-1, is like nuc-2 in that it fails to make the alkaline phosphatase or the permease referred to above. nuc-1 is epistatic to UW-6 in the double mutant. The control of phosphorus metabolism is discussed, and is compared with some other control systems in filamentous fungi.


2021 ◽  
Author(s):  
Morito Sakuma ◽  
Shingo Honda ◽  
Hiroshi Ueno ◽  
Kentaro Miyazaki ◽  
Nobuhiko Tokuriki ◽  
...  

Enzymes inherently exhibit molecule-to-molecule heterogeneity in catalytic activity or function, which underlies the acquisition of new functions in evolutionary processes. However, correlations between the functional heterogeneity of an enzyme and its multi-functionality or promiscuity remain elusive. In addition, the modulation of functional heterogeneity upon genetic perturbation is currently unexplored. Here, we quantitatively analyzed functional heterogeneity in the wild-type and 69 single-point mutants of Escherichia coli alkaline phosphatase (AP) by employing single-molecule assay with a femtoliter reactor array device. Most mutant enzymes exhibited higher functional heterogeneity than the wild-type enzyme, irrespective of catalytic activity. These results indicated that the wild-type AP minimizes functional heterogeneity, and single-point mutations can significantly expand the span of functional heterogeneity in AP. Moreover, we identified a clear correlation between functional heterogeneity and promiscuous activities. These findings suggest that enzymes can acquire greater functional heterogeneity following marginal genetic perturbations that concomitantly promote catalytic promiscuity.


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