Distribution of adenosine 5′-triphosphate (ATP)-dependent hexose kinases in microorganisms

Delvalle, J A; Asensio, Carlos

doi:10.1016/0303-2647(78)90008-4

Cited by 15 publications

(9 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Taking into account the different specificities of hexokinases in micro-organisms [15] and the data presented here, results obtained with undefined preparations of hexokinase [16] should be reconsidered.…”

Section: Discussionmentioning

confidence: 96%

Toxicity of 3‐O‐methyl glucose in yeast is due to its phosphorylation by glucokinase

Siverio¹,

Valdes-Hevia²,

Gancedo³

1986

FEBS Letters

View full text Add to dashboard Cite

3-O-Methyl glucose inhibited the growth of S.cerevisiae on non-fermentable carbon sources only in strains possessing glucokinase. Accumulation of a phosphorylated derivative of 3-O-methyl glucose occurred only in strains carrying glucokinase. Phosphorylation of the sugar in vitro was observed with partially purified preparations of glucokinase but not with equivalent preparations of isoenzymes PI or PI1 of hexokinase. The K,,, value of glucokinase for 3-O-methyl glucose was 5 mM and the I',,,, was N l/100 of that found for glucose. A mutant resistant to 3-O-methyl glucose was isolated from a strain possessing only glucokinase. This mutant had only about 10% of the glucokinase found in the parental strain. 3-O-Methyl glucoseGlucokinase Phosphorylation (Yeast) Hexokinase

show abstract

Section: Discussionmentioning

confidence: 96%

Toxicity of 3‐O‐methyl glucose in yeast is due to its phosphorylation by glucokinase

Siverio¹,

Valdes-Hevia²,

Gancedo³

1986

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…The kinetic characteristics of both activities are shown in Table 1. Both are hexokinases as they phosphorylate glucose, fructose and mannose; however, hexokinase 1 is clearly different from other hexokinases studied [20,21] as it presents a low affinity for glucose and some of its analogues. Hexokinase 2 behaves kinetically as a conventional hexokinase [20].…”

Section: Biochemical Characterization Of Hexokinases From S Pombementioning

confidence: 94%

Schizosaccharomyces pombe possesses an unusual and a conventional hexokinase: biochemical and molecular characterization of both hexokinases

Petit¹,

Blázquez²,

Gancedo³

1996

FEBS Letters

View full text Add to dashboard Cite

Two hexokinases were characterized in Schizosaccharomyces pombe: hexokinase 1, with a low phosphorylation coefficient on glucose (K m 8.5 mM) and hexokinase 2, a kinetically conventional hexokinase. Genes hxkl ÷ and hxk2 + encoding these enzymes were cloned and sequenced. Disruption of hxkl + had no effect on growth but disruption of hxk2 ÷ doubled the generation time in glucose. Spores carrying the double disruption hxkl ÷ hxk2 ÷ did not grow on glucose or fructose after one week. Expression of hxkl + increased strongly during growth in fructose or glycerol. Expression of hxk2 + was highest during growth in glycerol. A NADP-dependent glucose dehydrogenase was detected, but not a glucokinase.

show abstract

mentioning

confidence: 99%

“…It has been shown that prokaryotic kinases, like those of Streptococcus mutans, B. subtilis, Zymomonas mobilis, and Rhodospirillum rubrum, are chiefly glucose kinases (13,19,27), as only glucose phosphorylation activity was detected. Kinases characterized in Archaea, however, have been shown to have broad substrate specificity, phosphorylating glucose, mannose, fructose, and other sugars (14,18).…”

mentioning

confidence: 99%

“…Kinases characterized in Archaea, however, have been shown to have broad substrate specificity, phosphorylating glucose, mannose, fructose, and other sugars (14,18). Eukaryotic kinases, from yeast (13) to humans (19), have broad specificity and are capable of phosphorylating many hexoses (7), although phosphorylation of hexosamines was not tested. Broad-specificity kinases have not been characterized in many eubacteria.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Characterization of the RokA and HexA Broad-Substrate-Specificity Hexokinases from Bacteroides fragilis and Their Role in Hexose and N -Acetylglucosamine Utilization

Brigham

Malamy

2005

J Bacteriol

View full text Add to dashboard Cite

Bacteroides fragilis, a human gastrointestinal commensal and an opportunistic pathogen, utilizes simple and complex sugars and polysaccharides for growth in the large intestine and at sites of infection. Because B. fragilis lacks transport-linked sugar phosphorylation systems, cytoplasmic kinase(s) was expected to be required for the phosphorylation of hexoses and hexosamines. We have now identified two hexose kinases that are important for growth of B. fragilis on glucose, mannose, and other sugars. One kinase (RokA), a member of the ROK family of proteins, was found to be the sole kinase for activation of N-acetyl-D-glucosamine (NAG). The other kinase (HexA) is responsible for the majority of the glucose kinase activity in the cell, although a hexA deletion mutant strain was not defective for growth on any substrate tested. Deletion of both the rokA and hexA kinase genes resulted in inability of the cell to use glucose, mannose, NAG, and many other sugars. We purified RokA and determined its approximate molecular mass to be 36.5 kDa. The purified RokA protein was shown to phosphorylate several substrates, including glucose, NAG, and mannose, but not N-acetylmannosamine or N-acetylneuraminic acid. Phylogenetic analysis of RokA showed that it is most similar to kinases from the Cytophaga-Flavibacterium-Bacteroides group, while HexA was most similar to other bacterial hexokinases and eukaryotic hexokinases.The "nanaerobic" gram-negative organism Bacteroides fragilis (4) is capable of utilizing a wide variety of simple sugars and complex oligosaccharides as sources of carbon and energy for growth. This is a useful property for a bacterium that is both a gastrointestinal tract commensal and an opportunistic pathogen. In the large intestine, undigested dietary polysaccharides and host-derived glycoproteins, such as colonic mucin, can serve as growth substrates for B. fragilis (22). At sites of infection, the availability of host cell surface glycoproteins and glycolipids provides nutrients during the establishment phase and after abscess formation. As an example, the cell surface Lewis antigen contains galactose, mannose, N-acetyl-D-glucosamine (NAG), and N-acetylneuraminic acid (34, 46), all of which can serve as carbon and energy sources for B. fragilis. Godoy et al. (17) demonstrated that the B. fragilis neuraminidase (the product of the nanH gene) catalyzes the removal of terminal sialic acids from surface polysaccharides of CHO cells in monolayer cultures and in the rat granuloma pouch model system, both of which are glucose-limited growth conditions. Accordingly, ⌬nanH mutant strains are compromised for growth in these model systems. N-acetyl-D-glucosamine is an excellent carbon and energy source for B. fragilis and appears to be utilized more efficiently than glucose (8). Release of NAG from host glycoproteins and its transport into the cell can also influence anabolic cellular processes. NAG is a major component of the murein sacculus (21), and the ability to acquire or produce NAG affects cell wall product...

show abstract

Distribution of adenosine 5′-triphosphate (ATP)-dependent hexose kinases in microorganisms

Cited by 15 publications

References 34 publications

Toxicity of 3‐O‐methyl glucose in yeast is due to its phosphorylation by glucokinase

Toxicity of 3‐O‐methyl glucose in yeast is due to its phosphorylation by glucokinase

Schizosaccharomyces pombe possesses an unusual and a conventional hexokinase: biochemical and molecular characterization of both hexokinases

Characterization of the RokA and HexA Broad-Substrate-Specificity Hexokinases from Bacteroides fragilis and Their Role in Hexose and N -Acetylglucosamine Utilization

Contact Info

Product

Resources

About