PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
18533012-8	2008	Proteome analyses revealed distinct patterns in phosphorylation of hexokinase 2, glucokinase and enolase isoenzymes in the xylose- and glucose-grown cells.	Xylose	123-129	glucokinase	Saccharomyces cerevisiae S288C	81-92
18533012-8	2008	Proteome analyses revealed distinct patterns in phosphorylation of hexokinase 2, glucokinase and enolase isoenzymes in the xylose- and glucose-grown cells.	Glucose	135-142	glucokinase	Saccharomyces cerevisiae S288C	81-92
17428308-1	2007	We have studied how the lack of glucose sensors in the plasma membrane, or of the enzymes Hxk1, Hxk2, Glk1, which catalyze the first intracellular step in glucose metabolism, affect the different responses of Saccharomyces cerevisiae to glucose.	Glucose	155-162	glucokinase	Saccharomyces cerevisiae S288C	102-106
17428308-1	2007	We have studied how the lack of glucose sensors in the plasma membrane, or of the enzymes Hxk1, Hxk2, Glk1, which catalyze the first intracellular step in glucose metabolism, affect the different responses of Saccharomyces cerevisiae to glucose.	Glucose	155-162	glucokinase	Saccharomyces cerevisiae S288C	102-106
17428308-3	2007	In an hxk1 hxk2 glk1 strain, unable to phosphorylate glucose, all of these responses to the sugar were suppressed or strongly reduced.	Sugars	92-97	glucokinase	Saccharomyces cerevisiae S288C	16-20
15339905-9	2004	Glucose phosphorylation by glucokinase or the hexokinases is required for glucose-induced Ras2 GTP loading.	Glucose	0-7	glucokinase	Saccharomyces cerevisiae S288C	27-38
17573926-3	2007	Isolation of the permissive glucose-phosphorylating enzyme, mass spectrometric tryptic peptide analysis and determination of basic kinetic data identify a novel glucokinase (KlGlk1) encoded by ORF KLLA0C01,155g.	Glucose	28-35	glucokinase	Saccharomyces cerevisiae S288C	161-172
17573926-3	2007	Isolation of the permissive glucose-phosphorylating enzyme, mass spectrometric tryptic peptide analysis and determination of basic kinetic data identify a novel glucokinase (KlGlk1) encoded by ORF KLLA0C01,155g.	Peptides	87-94	glucokinase	Saccharomyces cerevisiae S288C	161-172
15339905-9	2004	Glucose phosphorylation by glucokinase or the hexokinases is required for glucose-induced Ras2 GTP loading.	Glucose	74-81	glucokinase	Saccharomyces cerevisiae S288C	27-38
11311123-2	2001	After shifting the cells to a non-fermentable carbon source, the HXK2 gene is repressed and the HXK1 and GLK1 genes are rapidly de-repressed, producing the enzymes hexokinase 1 (Hxk1p) and glucokinase (Glk1p) respectively.	Carbon	46-52	glucokinase	Saccharomyces cerevisiae S288C	105-109
12796298-3	2003	The yeast Saccharomyces cerevisiae has three enzymes (Hxk1p, Hxk2p, and Glk1p) that convert glucose to Glc-6-P.	Glucose	92-99	glucokinase	Saccharomyces cerevisiae S288C	72-77
12796298-3	2003	The yeast Saccharomyces cerevisiae has three enzymes (Hxk1p, Hxk2p, and Glk1p) that convert glucose to Glc-6-P.	Glucose-6-Phosphate	103-110	glucokinase	Saccharomyces cerevisiae S288C	72-77
12383517-0	2002	Cloning and characterization of glucokinase from a methylotrophic yeast Hansenula polymorpha: different effects on glucose repression in H. polymorpha and Saccharomyces cerevisiae.	Glucose	115-122	glucokinase	Saccharomyces cerevisiae S288C	32-43
12054864-1	2002	In the presence of glucose the protein hexokinase 2 (Hxk2p), normally resident in the cytosol, is translocated to the nucleus where it impairs the activation of transcription of the glucose-repressed genes HXK1, GLK1 and SUC2, and promotes the activation of transcription of the glucose-induced genes HXK2 and HXT1.	Glucose	19-26	glucokinase	Saccharomyces cerevisiae S288C	212-216
12054864-1	2002	In the presence of glucose the protein hexokinase 2 (Hxk2p), normally resident in the cytosol, is translocated to the nucleus where it impairs the activation of transcription of the glucose-repressed genes HXK1, GLK1 and SUC2, and promotes the activation of transcription of the glucose-induced genes HXK2 and HXT1.	Glucose	182-189	glucokinase	Saccharomyces cerevisiae S288C	212-216
12054864-1	2002	In the presence of glucose the protein hexokinase 2 (Hxk2p), normally resident in the cytosol, is translocated to the nucleus where it impairs the activation of transcription of the glucose-repressed genes HXK1, GLK1 and SUC2, and promotes the activation of transcription of the glucose-induced genes HXK2 and HXT1.	Glucose	182-189	glucokinase	Saccharomyces cerevisiae S288C	212-216
11311123-2	2001	After shifting the cells to a non-fermentable carbon source, the HXK2 gene is repressed and the HXK1 and GLK1 genes are rapidly de-repressed, producing the enzymes hexokinase 1 (Hxk1p) and glucokinase (Glk1p) respectively.	Carbon	46-52	glucokinase	Saccharomyces cerevisiae S288C	189-200
11311123-2	2001	After shifting the cells to a non-fermentable carbon source, the HXK2 gene is repressed and the HXK1 and GLK1 genes are rapidly de-repressed, producing the enzymes hexokinase 1 (Hxk1p) and glucokinase (Glk1p) respectively.	Carbon	46-52	glucokinase	Saccharomyces cerevisiae S288C	202-207
11311123-3	2001	Because the in vivo functions of the Hxk1p and Glk1p enzymes have remained a mystery so far, we have investigated this glucose-induced regulatory process.	Glucose	119-126	glucokinase	Saccharomyces cerevisiae S288C	47-52
11311123-4	2001	Here we demonstrate the involvement of Hxk2p in the glucose-induced repression of the HXK1 and GLK1 genes and the glucose-induced expression of the HXK2 gene.	Glucose	52-59	glucokinase	Saccharomyces cerevisiae S288C	95-99
11311123-6	2001	Further experimental evidence, using mutant cells expressing a truncated version of Hxk2p unable to enter the nucleus, shows that nuclear localization of Hxk2p is necessary for glucose-induced repression signalling of the HXK1 and GLK1 genes and for glucose-induced expression of the HXK2 gene.	Glucose	177-184	glucokinase	Saccharomyces cerevisiae S288C	231-235
11311123-6	2001	Further experimental evidence, using mutant cells expressing a truncated version of Hxk2p unable to enter the nucleus, shows that nuclear localization of Hxk2p is necessary for glucose-induced repression signalling of the HXK1 and GLK1 genes and for glucose-induced expression of the HXK2 gene.	Glucose	250-257	glucokinase	Saccharomyces cerevisiae S288C	231-235
11311123-7	2001	Gel mobility-shift analysis shows that Hxk2p-mediated regulation is exerted through ERA (ethanol repression autoregulation)-like regulatory sequences present in the HXK1 and GLK1 promoters and in two downstream repressing sequences of the HXK2 gene.	Ethanol	89-96	glucokinase	Saccharomyces cerevisiae S288C	174-178
10510295-1	1999	The glucokinase gene GLK1 of the yeast Saccharomyces cerevisiae is transcriptionally regulated in response to the carbon source of the growth medium.	Carbon	114-120	glucokinase	Saccharomyces cerevisiae S288C	4-15
10510295-1	1999	The glucokinase gene GLK1 of the yeast Saccharomyces cerevisiae is transcriptionally regulated in response to the carbon source of the growth medium.	Carbon	114-120	glucokinase	Saccharomyces cerevisiae S288C	21-25
10510295-2	1999	Northern-blot analysis shows that the GLK1 gene is expressed at a basal level in the presence of glucose, de-repressed more than 6-fold under conditions of sugar limitation and more than 25-fold under conditions of ethanol induction.	Glucose	97-104	glucokinase	Saccharomyces cerevisiae S288C	38-42
10510295-2	1999	Northern-blot analysis shows that the GLK1 gene is expressed at a basal level in the presence of glucose, de-repressed more than 6-fold under conditions of sugar limitation and more than 25-fold under conditions of ethanol induction.	Sugars	156-161	glucokinase	Saccharomyces cerevisiae S288C	38-42
10510295-2	1999	Northern-blot analysis shows that the GLK1 gene is expressed at a basal level in the presence of glucose, de-repressed more than 6-fold under conditions of sugar limitation and more than 25-fold under conditions of ethanol induction.	Ethanol	215-222	glucokinase	Saccharomyces cerevisiae S288C	38-42
10510295-5	1999	Secondly, an ethanol repression autoregulation (ERA)/twelve-fold TA repeat (TAB) repressor element was identified within the promoter region of the GLK1 gene.	Ethanol	13-20	glucokinase	Saccharomyces cerevisiae S288C	148-152
10510295-10	1999	In order to achieve the severe glucose repression of GLK1, constitutive repressor factors acting through the ERA/TAB element must counteract constitutive activation generated by Gcr1 binding to the GCR1 element.	Glucose	31-38	glucokinase	Saccharomyces cerevisiae S288C	53-57
10510295-12	1999	The combinatorial effect of the entire region leads to the regulated transcription of GLK1, i.e., silent in media with glucose and other preferred carbon sources, such as fructose or mannose, and increased levels of expression upon glucose depletion.	Glucose	119-126	glucokinase	Saccharomyces cerevisiae S288C	86-90
10510295-12	1999	The combinatorial effect of the entire region leads to the regulated transcription of GLK1, i.e., silent in media with glucose and other preferred carbon sources, such as fructose or mannose, and increased levels of expression upon glucose depletion.	Carbon	147-153	glucokinase	Saccharomyces cerevisiae S288C	86-90
10510295-12	1999	The combinatorial effect of the entire region leads to the regulated transcription of GLK1, i.e., silent in media with glucose and other preferred carbon sources, such as fructose or mannose, and increased levels of expression upon glucose depletion.	Fructose	171-179	glucokinase	Saccharomyces cerevisiae S288C	86-90
10510295-12	1999	The combinatorial effect of the entire region leads to the regulated transcription of GLK1, i.e., silent in media with glucose and other preferred carbon sources, such as fructose or mannose, and increased levels of expression upon glucose depletion.	Mannose	183-190	glucokinase	Saccharomyces cerevisiae S288C	86-90
10510295-12	1999	The combinatorial effect of the entire region leads to the regulated transcription of GLK1, i.e., silent in media with glucose and other preferred carbon sources, such as fructose or mannose, and increased levels of expression upon glucose depletion.	Glucose	232-239	glucokinase	Saccharomyces cerevisiae S288C	86-90
10217505-2	1999	The phosphorylation of glucose or fructose is catalysed by hexokinase PI (Hxk1), hexokinase PII (Hxk2) and a specific glucokinase (Glk1).	Glucose	23-30	glucokinase	Saccharomyces cerevisiae S288C	131-135
19402252-0	1999	Tuber-specific expression of a yeast invertase  and a bacterial glucokinase in potato leads to an activation  of sucrose phosphate synthase and the creation  of a sucrose futile cycle.	Sucrose	113-120	glucokinase	Saccharomyces cerevisiae S288C	64-75
10217505-2	1999	The phosphorylation of glucose or fructose is catalysed by hexokinase PI (Hxk1), hexokinase PII (Hxk2) and a specific glucokinase (Glk1).	Fructose	34-42	glucokinase	Saccharomyces cerevisiae S288C	131-135
8501032-1	1993	Glucose phosphorylation capacity is known to be in excess of glucose flux in Saccharomyces cerevisiae wild type but not in a mutant strain lacking the two hexokinases but still having glucokinase.	Glucose	0-7	glucokinase	Saccharomyces cerevisiae S288C	184-195
8917466-6	1996	An initial rapid response is mediated through any kinase, including Glk1, which is able to phosphorylate the available sugar.	Sugars	119-124	glucokinase	Saccharomyces cerevisiae S288C	68-72
8917466-8	1996	Both HXK1 and GLK1 are repressed upon addition of glucose or fructose.	Glucose	50-57	glucokinase	Saccharomyces cerevisiae S288C	14-18
8917466-8	1996	Both HXK1 and GLK1 are repressed upon addition of glucose or fructose.	Fructose	61-69	glucokinase	Saccharomyces cerevisiae S288C	14-18
7730377-2	1995	Glucokinase is distinguished from yeast hexokinase and low Km mammalian hexokinases by its low affinity for glucose and its cooperative behavior, even though glucose binding residues and catalytic residues are highly conserved in all of these forms of hexokinase.	Glucose	108-115	glucokinase	Saccharomyces cerevisiae S288C	0-11
7730377-2	1995	Glucokinase is distinguished from yeast hexokinase and low Km mammalian hexokinases by its low affinity for glucose and its cooperative behavior, even though glucose binding residues and catalytic residues are highly conserved in all of these forms of hexokinase.	Glucose	158-165	glucokinase	Saccharomyces cerevisiae S288C	0-11
9580251-9	1998	The intracellular glucose level rose in 5 min after addition of 100 mM-glucose to 0.5-2 mM in the wild-type strain, +/- 10 mM in a hxk1 delta hxk2 delta glk1 delta and 2-3 mM in a tps1 delta strain.	Glucose	18-25	glucokinase	Saccharomyces cerevisiae S288C	153-157
7732723-3	1995	In this paper, we describe the transcriptional regulation of the HXK1, HXK2 and GLK1 genes in the hope of revealing differences in the steady-state levels of mRNA associated with a particular carbon source used in the culture medium.	Carbon	192-198	glucokinase	Saccharomyces cerevisiae S288C	80-84
8501032-3	1993	The glucokinase-dependent strain accumulates substantial amounts of glucose internally in batch culture after exhaustion of glucose, as well as from maltose.	Glucose	68-75	glucokinase	Saccharomyces cerevisiae S288C	4-15
8501032-3	1993	The glucokinase-dependent strain accumulates substantial amounts of glucose internally in batch culture after exhaustion of glucose, as well as from maltose.	Glucose	124-131	glucokinase	Saccharomyces cerevisiae S288C	4-15
8501032-3	1993	The glucokinase-dependent strain accumulates substantial amounts of glucose internally in batch culture after exhaustion of glucose, as well as from maltose.	Maltose	149-156	glucokinase	Saccharomyces cerevisiae S288C	4-15
8501032-5	1993	Furthermore, in contrast to activity of hexokinase and other enzymes, little glucokinase activity is revealed by toluene treatment of cells.	Toluene	113-120	glucokinase	Saccharomyces cerevisiae S288C	77-88
8501032-6	1993	These results may point to a connection between glucose entry and its phosphorylation by glucokinase, but separate explanations for the various findings are also possible.	Glucose	48-55	glucokinase	Saccharomyces cerevisiae S288C	89-100
1322708-10	1992	Experiments with yeast strains carrying point or deletion mutations in the genes coding for the sugar phosphorylating enzymes hexokinase PI and PII and glucokinase showed that activation of the H(+)-ATPase with glucose or fructose was completely dependent on the presence of a kinase able to phosphorylate the sugar.	Sugars	96-101	glucokinase	Saccharomyces cerevisiae S288C	126-163
1322708-10	1992	Experiments with yeast strains carrying point or deletion mutations in the genes coding for the sugar phosphorylating enzymes hexokinase PI and PII and glucokinase showed that activation of the H(+)-ATPase with glucose or fructose was completely dependent on the presence of a kinase able to phosphorylate the sugar.	Glucose	211-218	glucokinase	Saccharomyces cerevisiae S288C	126-163
1322708-10	1992	Experiments with yeast strains carrying point or deletion mutations in the genes coding for the sugar phosphorylating enzymes hexokinase PI and PII and glucokinase showed that activation of the H(+)-ATPase with glucose or fructose was completely dependent on the presence of a kinase able to phosphorylate the sugar.	Fructose	222-230	glucokinase	Saccharomyces cerevisiae S288C	126-163
1322708-10	1992	Experiments with yeast strains carrying point or deletion mutations in the genes coding for the sugar phosphorylating enzymes hexokinase PI and PII and glucokinase showed that activation of the H(+)-ATPase with glucose or fructose was completely dependent on the presence of a kinase able to phosphorylate the sugar.	Sugars	310-315	glucokinase	Saccharomyces cerevisiae S288C	126-163
1868842-16	1991	To verify the role of hexokinases in glucose repression, the third glucose-phosphorylating enzyme, glucokinase, was stably overexpressed in a hexokinase PI/PII double-null mutant.	Glucose	67-74	glucokinase	Saccharomyces cerevisiae S288C	99-110
1496915-4	1992	Fructose 1-phosphate antagonizes this inhibition by causing dissociation of the glucokinase-regulatory protein complex.	fructose-1-phosphate	0-20	glucokinase	Saccharomyces cerevisiae S288C	80-91
3072253-0	1988	Structure of yeast glucokinase, a strongly diverged specific aldo-hexose-phosphorylating isoenzyme.	aldo-hexose	61-72	glucokinase	Saccharomyces cerevisiae S288C	19-30
1874414-6	1991	The strain lacking both hexokinases and containing glucokinase was an exception in having reduced flux, a result fitting with its maximal rate of glucose phosphorylation in vitro.	Glucose	146-153	glucokinase	Saccharomyces cerevisiae S288C	51-62
3072253-1	1988	Saccharomyces cerevisiae glucokinase (GLK) is the only described hexose-phosphorylating enzyme specific for aldo-hexoses.	Hexoses	65-71	glucokinase	Saccharomyces cerevisiae S288C	25-36
3072253-1	1988	Saccharomyces cerevisiae glucokinase (GLK) is the only described hexose-phosphorylating enzyme specific for aldo-hexoses.	Hexoses	65-71	glucokinase	Saccharomyces cerevisiae S288C	38-41
3072253-14	1988	In both GLK and the hexokinases, a lysine residue is also conserved at aa position 110 which probably corresponds to the ATP-binding site.	Lysine	35-41	glucokinase	Saccharomyces cerevisiae S288C	8-11
3072253-14	1988	In both GLK and the hexokinases, a lysine residue is also conserved at aa position 110 which probably corresponds to the ATP-binding site.	Adenosine Triphosphate	121-124	glucokinase	Saccharomyces cerevisiae S288C	8-11
3072253-15	1988	Additionally, a consensus sequence of 8 aa residues which is common for ATP-binding enzymes is conserved within the C-terminal part of GLK.	Adenosine Triphosphate	72-75	glucokinase	Saccharomyces cerevisiae S288C	135-138
3540605-3	1986	Mutant strains without any hexokinase can still grow on glucose by using a third enzyme, glucokinase.	Glucose	56-63	glucokinase	Saccharomyces cerevisiae S288C	89-100
2831059-4	1988	Experiments with double and triple mutants in hexokinase 1, hexokinase 2 or glucokinase indicated that the presence of one of the three kinases was both necessary and enough for induction of the cAMP signal by glucose and the presence of one of the two hexokinases necessary and enough for induction by fructose.	Cyclic AMP	195-199	glucokinase	Saccharomyces cerevisiae S288C	76-87
2831059-4	1988	Experiments with double and triple mutants in hexokinase 1, hexokinase 2 or glucokinase indicated that the presence of one of the three kinases was both necessary and enough for induction of the cAMP signal by glucose and the presence of one of the two hexokinases necessary and enough for induction by fructose.	Glucose	210-217	glucokinase	Saccharomyces cerevisiae S288C	76-87
2831059-4	1988	Experiments with double and triple mutants in hexokinase 1, hexokinase 2 or glucokinase indicated that the presence of one of the three kinases was both necessary and enough for induction of the cAMP signal by glucose and the presence of one of the two hexokinases necessary and enough for induction by fructose.	Fructose	303-311	glucokinase	Saccharomyces cerevisiae S288C	76-87
3298207-1	1987	Wild-type Saccharomyces cerevisiae organisms contain three kinases which catalyze the phosphorylation of glucose: two hexokinase isozymes (PI and PII) and one glucokinase.	Glucose	105-112	glucokinase	Saccharomyces cerevisiae S288C	159-170
3533151-1	1986	Incubation of Saccharomyces cerevisiae with xylose and ethanol for 16 hours leads to a decrease of hexokinase (and glucokinase) activity in the cells.	Xylose	44-50	glucokinase	Saccharomyces cerevisiae S288C	115-126
3533151-1	1986	Incubation of Saccharomyces cerevisiae with xylose and ethanol for 16 hours leads to a decrease of hexokinase (and glucokinase) activity in the cells.	Ethanol	55-62	glucokinase	Saccharomyces cerevisiae S288C	115-126
6341351-1	1983	Genes complementing the glucose-negative fructose-negative Saccharomyces cerevisiae triple mutant strain (hxkl hxk2 glk1), which lacks hexokinase PI, hexokinase PII, and glucokinase, were obtained from a pool of yeast DNA in the multicopy plasmid YEp13.	Glucose	24-31	glucokinase	Saccharomyces cerevisiae S288C	116-120
3906028-2	1985	Variations in the amounts of these enzymes in cells growing on glucose and on ethanol showed that hexokinase PI was a constitutive enzyme, whereas synthesis of hexokinase PII and glucokinase were regulated by the carbon source used.	Glucose	63-70	glucokinase	Saccharomyces cerevisiae S288C	179-190
3906028-2	1985	Variations in the amounts of these enzymes in cells growing on glucose and on ethanol showed that hexokinase PI was a constitutive enzyme, whereas synthesis of hexokinase PII and glucokinase were regulated by the carbon source used.	Ethanol	78-85	glucokinase	Saccharomyces cerevisiae S288C	179-190
3906028-2	1985	Variations in the amounts of these enzymes in cells growing on glucose and on ethanol showed that hexokinase PI was a constitutive enzyme, whereas synthesis of hexokinase PII and glucokinase were regulated by the carbon source used.	Carbon	213-219	glucokinase	Saccharomyces cerevisiae S288C	179-190
3906028-3	1985	Glucokinase proved to be a glucomannokinase with Km values of 0.04 mM for both glucose and mannose.	Glucose	79-86	glucokinase	Saccharomyces cerevisiae S288C	0-11
3906028-3	1985	Glucokinase proved to be a glucomannokinase with Km values of 0.04 mM for both glucose and mannose.	Mannose	91-98	glucokinase	Saccharomyces cerevisiae S288C	0-11
3906028-6	1985	Glucokinase was protected by ATP from this inactivation.	Adenosine Triphosphate	29-32	glucokinase	Saccharomyces cerevisiae S288C	0-11
3906028-7	1985	D-Xylose acted as a competitive inhibitor of hexokinase PI and glucokinase and as a non-competitive inhibitor of hexokinase PII.	Xylose	0-8	glucokinase	Saccharomyces cerevisiae S288C	45-74
6357942-1	1983	Mutants of Saccharomyces cerevisiae lacking glucokinase (EC 2.7.1.2) have no discernible phenotypic difference from the wild-type strain; in a hexokinaseless background, however, they are unable to grow on any sugar except galactose.	Sugars	210-215	glucokinase	Saccharomyces cerevisiae S288C	44-55
6357942-1	1983	Mutants of Saccharomyces cerevisiae lacking glucokinase (EC 2.7.1.2) have no discernible phenotypic difference from the wild-type strain; in a hexokinaseless background, however, they are unable to grow on any sugar except galactose.	Galactose	223-232	glucokinase	Saccharomyces cerevisiae S288C	44-55
6357942-3	1983	Spontaneous revertants of hxk1 hxk2 glk1 strains collected on glucose regain any one of these three enzymes.	Glucose	62-69	glucokinase	Saccharomyces cerevisiae S288C	36-40
6357942-9	1983	The location of GLK1 on chromosome III was indicated by loss of this chromosome when hexokinaseless diploids heterozygous for glk1 were selected for resistance to 2-deoxyglucose; the homologue of chromosome III carrying GLK1, the mating-type allele and other nutritional markers on this chromosome was lost.	Deoxyglucose	163-177	glucokinase	Saccharomyces cerevisiae S288C	16-20
32108112-5	2020	Polymerization inhibits enzymatic activity; the Glk1 monomer-polymer equilibrium sets a maximum rate of glucose phosphorylation regardless of Glk1 concentration.	Glucose	104-111	glucokinase	Saccharomyces cerevisiae S288C	48-52
6300872-9	1983	Low Km uptake was restored to the triple mutant by introduction of the cloned wild-type genes: HXK1 or HXK2, for fructose uptake, and HXK1, HXK2, or GLK1, for glucose uptake.	Glucose	159-166	glucokinase	Saccharomyces cerevisiae S288C	149-153
340926-1	1977	When strains of Saccharomyces cerevisiae carrying a single glucose-phosphorylating enzyme such as hexokinase Pl or hexokinase P2 or glucokinase, are subjected to the selection pressure against the toxic sugar 2-deoxyglucose, the majority of survivors are mutants lacking the respective enzymes.	Glucose	59-66	glucokinase	Saccharomyces cerevisiae S288C	115-143
340926-1	1977	When strains of Saccharomyces cerevisiae carrying a single glucose-phosphorylating enzyme such as hexokinase Pl or hexokinase P2 or glucokinase, are subjected to the selection pressure against the toxic sugar 2-deoxyglucose, the majority of survivors are mutants lacking the respective enzymes.	sugar 2-deoxyglucose	203-223	glucokinase	Saccharomyces cerevisiae S288C	115-143
32948893-5	2020	Here we revisit the role of the three hexose kinases, Hxk1, Hxk2 and Glk1, in glucose de/repression.	Glucose	78-85	glucokinase	Saccharomyces cerevisiae S288C	69-73
32612591-3	2020	Sequence comparison with Saccharomyces cerevisiae identified four enzymes (Hxk1, Hxk2, Glk1, and Glk4) in C. albicans with putative roles in sugar phosphorylation.	Sugars	141-146	glucokinase	Saccharomyces cerevisiae S288C	87-91
32108112-7	2020	Yeast containing nonpolymerizing Glk1 were less fit when growing on sugars and more likely to die when refed glucose.	Glucose	109-116	glucokinase	Saccharomyces cerevisiae S288C	33-37
30397769-7	2019	Transcription analysis revealed that the expression levels of INU1 for inulinase and GLK1 for glucokinase in Kmrag5 were higher than those in the parental strain; the expression level of INU1 in Kmmig1 was higher, but the expression levels of RAG1 for a low-affinity glucose transporter in Kmmig1 and Kmrag5 were lower.	Glucose	267-274	glucokinase	Saccharomyces cerevisiae S288C	85-89
19743421-4	2009	Significant increases in the levels of five proteins involved in glycolysis and alcohol biosynthesis pathways (e.g. Glk1p, Fba1p, Eno1p, Pdc1p and Adh1p) might play critical roles in improving ethanol productivity of the fermentation process and shortening the fermentation time when inoculation sizes were increased.	Alcohols	80-87	glucokinase	Saccharomyces cerevisiae S288C	116-121
19743421-4	2009	Significant increases in the levels of five proteins involved in glycolysis and alcohol biosynthesis pathways (e.g. Glk1p, Fba1p, Eno1p, Pdc1p and Adh1p) might play critical roles in improving ethanol productivity of the fermentation process and shortening the fermentation time when inoculation sizes were increased.	Ethanol	193-200	glucokinase	Saccharomyces cerevisiae S288C	116-121
29422502-5	2018	Genome sequencing of the evolved mutant followed by CRISPR/Cas9-based reverse engineering revealed that mutations in the glucose phosphorylating enzymes (Hxk1, Hxk2, Glk1) were sufficient to confer simultaneous glucose and xylose utilization.	Glucose	121-128	glucokinase	Saccharomyces cerevisiae S288C	166-170
29422502-5	2018	Genome sequencing of the evolved mutant followed by CRISPR/Cas9-based reverse engineering revealed that mutations in the glucose phosphorylating enzymes (Hxk1, Hxk2, Glk1) were sufficient to confer simultaneous glucose and xylose utilization.	Glucose	211-218	glucokinase	Saccharomyces cerevisiae S288C	166-170
29422502-5	2018	Genome sequencing of the evolved mutant followed by CRISPR/Cas9-based reverse engineering revealed that mutations in the glucose phosphorylating enzymes (Hxk1, Hxk2, Glk1) were sufficient to confer simultaneous glucose and xylose utilization.	Xylose	223-229	glucokinase	Saccharomyces cerevisiae S288C	166-170
19834894-4	2009	The expression levels of 20 enzymes in glucose fermentation and 5 enzymes in the tricarboxylic acid cycle were reduced by furfural, with notably delayed temporal downregulations of Glk1p, Tdh1p, Eno1p and Aco1p, which is correlated to the reduced ethanol formation rate and glucose consumption rate by 66.7 and 60.4%, respectively.	Furaldehyde	122-130	glucokinase	Saccharomyces cerevisiae S288C	181-186
19834894-4	2009	The expression levels of 20 enzymes in glucose fermentation and 5 enzymes in the tricarboxylic acid cycle were reduced by furfural, with notably delayed temporal downregulations of Glk1p, Tdh1p, Eno1p and Aco1p, which is correlated to the reduced ethanol formation rate and glucose consumption rate by 66.7 and 60.4%, respectively.	Ethanol	247-254	glucokinase	Saccharomyces cerevisiae S288C	181-186
19834894-4	2009	The expression levels of 20 enzymes in glucose fermentation and 5 enzymes in the tricarboxylic acid cycle were reduced by furfural, with notably delayed temporal downregulations of Glk1p, Tdh1p, Eno1p and Aco1p, which is correlated to the reduced ethanol formation rate and glucose consumption rate by 66.7 and 60.4%, respectively.	Glucose	274-281	glucokinase	Saccharomyces cerevisiae S288C	181-186