UTILIZATION OF L-Α-Glycerophosphate BY ESCHERICHIA COLI WITHOUT HYDROLYSIS

Lin, E. C. C.; Koch, James P.; Chused, Thomas M.; Jorgensen, Sally E.

doi:10.1073/pnas.48.12.2145

Cited by 120 publications

(57 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The main pathway for glycerol utilization involves a glycerol kinase (GK) (E.C.2.7.1.30) which phosphorylates glycerol to glycerol-3-phosphate (G3P), and NAD-independent G3P dehydrogenase (NADi-G3PDH) (E.C.1.1.99.5) which oxidizes G3P to dihydroxyacetone phosphate. This pathway has been reported in Bacillus subtilis (Mindich 1968 ;Lindgren and Rutberg 1974), Pseudomonas aeruginosa (Heath and Gaudy 1978), Rhodopseudomonas capsulata (Pike 1982), Rhodopseudomonas sphaeroides (Pike and Sojka 1975) and aerobically grown Escherichia coli (Lin et al 1962 ;Koch et al 1964).…”

Section: Introductionmentioning

confidence: 64%

Characterization of glycerol kinase and NAD-independent glycerol-3-phosphate dehydrogenase from Pediococcus pentosaceus N5p

Pasteris

Saad

1998

Lett Appl Microbiol

View full text Add to dashboard Cite

S A AD . 1998. The pathway involved in glycerol dissimilation in Pediococcus pentosaceus N5p, a strain isolated from wine, includes glycerol kinase and NAD-independent glycerol-3P dehydrogenase. The properties of these enzymes were studied. Glycerol kinase activity was maximal at 28°C and pH 7·5 in 50 mmol l −1 TrisHCl buffer. The end-products of the reaction acted as competitive inhibitors while fructose-1,6-diphosphate was a non-competitive inhibitor. Mg 2+ was required for optimal enzyme activity. The Km values for both substrates were 0·11 and 0·37 mmol l −1 for glycerol and ATP, respectively. NAD-independent glycerol-3P dehydrogenase activity was maximal at 37°C and pH 7·5 in 100 mmol l −1 Tris-HCl buffer. The enzymatic activity was activated by KCN and bivalent cations as Mg 2+ and Ca 2+, but it was strongly inhibited by others. Dihydroxyacetone phosphate acted as competitive inhibitor while ATP and phosphenolpyruvate were non-competitive inhibitors.

show abstract

Section: Introductionmentioning

confidence: 64%

Characterization of glycerol kinase and NAD-independent glycerol-3-phosphate dehydrogenase from Pediococcus pentosaceus N5p

Pasteris

Saad

1998

Lett Appl Microbiol

View full text Add to dashboard Cite

show abstract

“…After 2 h incubation, samples were Lin (1973) but with the buffer at pH 9-0 instead of 9.5. G3P dehydrogenase was measured as described by Lin et al (1962). The amount of protein was determined by the Lowry method, with bovine serum albumin as standard.…”

Section: Methodsmentioning

confidence: 99%

Glycerol catabolism in Bacillus subtilis: nucleotide sequence of the genes encoding glycerol kinase (glpK) and glycerol-3-phosphate dehydrogenase (glpD)

Holmberg

Beijer²,

Rutberg³

et al. 1990

Journal of General Microbiology

View full text Add to dashboard Cite

The glpPKD region of the Bacillus subtilis chromosome was cloned in its natural host in plasmid pHPl3. The glpPKD region contains genes required for glycerol catabolism: glpK coding for glycerol kinase, glpD coding for glycerol-3-phosphate (G3P) dehydrogenase and glpP, proposed to code for a positively acting regulatory protein.The cloned 7 kb fragment carries wild-type alleles of glpK, glpD and glpP. It can also complement a strain deleted for the entire glpPKD region. The wild-type alleles were mapped to different subfragments, establishing the gene order glpP-glpK-glpD. The nucleotide sequence of glpK and glpD was determined. Immediately upstream of glpK, an additional open reading frame was found, possibly being part of the same operon. Putative transcription terminators were found in the region between glpK and glpD and downstream of glpD. In a coupled in vi&u transcriptionltranslation system, two proteins were found, corresponding in size to those predicted from the deduced amino acid sequences of glycerol kinase and G3P dehydrogenase (54 kDa and 63 kDa, respectively).

show abstract

“…(1962). Arginase (EC 3.5.3.1 ; L-arginine amidinohydrolase) was assayed according to the method of Middelhoven (1964), except that the urea produced was estimated by the diacetyl monoxime method of Moore & Kauffman (1970 …”

Section: Methodsmentioning

confidence: 99%

The Physiology of Mutants Derepressed for Sporulation in Saccharomyces cerevisiae

Vezinhet

Kinnaird

Dawes

1979

Journal of General Microbiology

View full text Add to dashboard Cite

1The spd I mutants of Saccharomyces cerevisiae are affected in the initiation of sporulation since they sporulate under conditions in which the wild-type does not. They are unable to grow on a range of non-fermentable carbon substrates, but can grow on ethanol. On others, including acetate, glycerol, lactate and pyruvate, the mutants sporulate abundantly, even in rich media. The mutation does not affect the uptake of glycerol or the synthesis of the enzymes concerned with its entry into general metabolic pathways. It probably affects a central metabolic function concerned with the metabolism of some, but not all, nonfermentable carbon sources. The spd I mutation is also expressed in haploids. When haploid or diploid cells are transferred to media containing only non-fermentable carbon substrates they become arrested in the G1 phase of the cell cycle before, or at, the execution point for the cdc 28 mutation. In diploids homozygous for the spd I gene these conditions also lead to a lowering of the repression by the nitrogen source. The spd I mutants are therefore probably not affected directly in events unique to the initiation of sporulation, but in areas of metabolism closely connected with both the arrest of cells in the GI phase of the cell cycle and the control of induction of sporulation. I N T R O D U C T I O NMutants of Saccharomyces cerevisiae which are derepressed for sporulation have been described previously (Dawes, 1975) ; these sporulate under certain conditions in which the wild-type does not. Those affected in a gene designated s p d l sporulate after reaching stationary phase on media containing glucose as carbon source, but unlike the wild-type, sporulation is initiated immediately when they are resuspended in a complete medium containing glycerol as the carbon source. The sporulation of these mutants is not altered by the mutation insofar as the duration of the process, the sequence of events, the number of spores per ascus and the viability of spores is concerned, and they appear to be modified in a metabolic or control function involved only in the initiation of sporulation.Initiation is a complex of metabolic and genetic events. It requires at least the presence of a and a mating-type alleles, the arrest of cell growth in the G1 stage of the cell division cycle and the specific derepression of sporulation. While growth and sporulation are exclusive processes, the arrest of vegetative growth is not necessarily followed by the induction of sporulation, since this is specifically repressed by controls dependent on some form of glucose repression (Miller, 1963 ; Vezinhet, 1970) and of nitrogen repression (Miller, 1963 ; Piiion, 1977). Moreover, cells can only switch to alternative development processes if they are in the G1 stage of the cell cycle (between cytokinesis and the initiation of DNA synthesis). Reid & Hartwell (1977) showed with haploid strains that the transition between the mitotic cell cycle and the two other processes of mating, and of entry into

show abstract

UTILIZATION OF L-Α-Glycerophosphate BY ESCHERICHIA COLI WITHOUT HYDROLYSIS

Cited by 120 publications

References 14 publications

Characterization of glycerol kinase and NAD-independent glycerol-3-phosphate dehydrogenase from Pediococcus pentosaceus N5p

Characterization of glycerol kinase and NAD-independent glycerol-3-phosphate dehydrogenase from Pediococcus pentosaceus N5p

Glycerol catabolism in Bacillus subtilis: nucleotide sequence of the genes encoding glycerol kinase (glpK) and glycerol-3-phosphate dehydrogenase (glpD)

The Physiology of Mutants Derepressed for Sporulation in Saccharomyces cerevisiae

Contact Info

Product

Resources

About