PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
2077946-1	1990	The enzyme acetohydroxy acid synthase (AHAS, EC 4.1.3.18) catalyzes two competing reactions of physiological importance: condensation of two molecules of pyruvate to form acetolactate (AL) or condensation of pyruvate and 2-ketobutyrate to form acetohydroxybutyrate (AHB).	alpha-acetolactate	171-183	ilvB acetolactate synthase like	Homo sapiens	39-43
2077946-1	1990	The enzyme acetohydroxy acid synthase (AHAS, EC 4.1.3.18) catalyzes two competing reactions of physiological importance: condensation of two molecules of pyruvate to form acetolactate (AL) or condensation of pyruvate and 2-ketobutyrate to form acetohydroxybutyrate (AHB).	alpha-acetolactate	185-187	ilvB acetolactate synthase like	Homo sapiens	39-43
2077946-2	1990	The activity of AHAS is most frequently analyzed using the Westerfeld method, in which the acetoin formed upon decarboxylation of AL is determined by colorimetric reaction with creatine and alpha-naphthol.	alpha-acetolactate	130-132	ilvB acetolactate synthase like	Homo sapiens	16-20
24965182-7	2015	The results confirm the role of the Ilv6 subunit in controlling alpha-acetolactate/diacetyl concentration and indicate no functional divergence between the two forms of Ilv6.	alpha-acetolactate	64-82	acetolactate synthase regulatory subunit	Saccharomyces cerevisiae S288C	36-40
3003115-3	1986	Previous data have shown that transcription of the ilvC gene is induced by the acetohydroxy acid isomeroreductase substrates, acetohydroxybutyrate or acetolactate, and that this substrate induction of ilvC expression is mediated by a positive activator encoded by the ilvY gene.	alpha-acetolactate	150-162	transcriptional regulator IlvY	Salmonella enterica subsp. enterica serovar Typhimurium str. LT2	268-272
2345154-1	1990	Acetohydroxy acid synthase (AHAS; EC 4.1.3.18) catalyzes the following two parallel, physiologically important reactions: condensation of two molecules of pyruvate to form acetolactate (AL), in the pathway to valine and leucine, and condensation of pyruvate plus 2-ketobutyrate to form acetohydroxybutyrate (AHB), in the pathway to isoleucine.	alpha-acetolactate	172-184	ilvB acetolactate synthase like	Homo sapiens	0-26
2345154-1	1990	Acetohydroxy acid synthase (AHAS; EC 4.1.3.18) catalyzes the following two parallel, physiologically important reactions: condensation of two molecules of pyruvate to form acetolactate (AL), in the pathway to valine and leucine, and condensation of pyruvate plus 2-ketobutyrate to form acetohydroxybutyrate (AHB), in the pathway to isoleucine.	alpha-acetolactate	172-184	ilvB acetolactate synthase like	Homo sapiens	28-32
2345154-1	1990	Acetohydroxy acid synthase (AHAS; EC 4.1.3.18) catalyzes the following two parallel, physiologically important reactions: condensation of two molecules of pyruvate to form acetolactate (AL), in the pathway to valine and leucine, and condensation of pyruvate plus 2-ketobutyrate to form acetohydroxybutyrate (AHB), in the pathway to isoleucine.	alpha-acetolactate	186-188	ilvB acetolactate synthase like	Homo sapiens	0-26
2345154-1	1990	Acetohydroxy acid synthase (AHAS; EC 4.1.3.18) catalyzes the following two parallel, physiologically important reactions: condensation of two molecules of pyruvate to form acetolactate (AL), in the pathway to valine and leucine, and condensation of pyruvate plus 2-ketobutyrate to form acetohydroxybutyrate (AHB), in the pathway to isoleucine.	alpha-acetolactate	186-188	ilvB acetolactate synthase like	Homo sapiens	28-32
24965182-8	2015	The greater contribution of the S. cerevisiae ILV6 to acetolactate production in natural brewing yeast hybrids appears rather to be due to higher levels of transcription relative to the S. eubayanus form.	alpha-acetolactate	54-66	acetolactate synthase regulatory subunit	Saccharomyces cerevisiae S288C	46-50
15958189-1	2005	Acetohydroxy acid synthase (AHAS) and related enzymes catalyze the production of chiral compounds [(S)-acetolactate, (S)-acetohydroxybutyrate, or (R)-phenylacetylcarbinol] from achiral substrates (pyruvate, 2-ketobutyrate, or benzaldehyde).	alpha-acetolactate	99-115	ilvB acetolactate synthase like	Homo sapiens	0-26
20504042-1	2010	Acetohydroxy acid synthase (AHAS) is a thiamin diphosphate-dependent enzyme that catalyzes the condensation of pyruvate with either another pyruvate molecule (product acetolactate) or 2-ketobutyrate (product acetohydroxybutyrate) as the first common step in the biosynthesis of branched-chain amino acids in plants, bacteria, algae, and fungi.	alpha-acetolactate	167-179	ilvB acetolactate synthase like	Homo sapiens	28-32
23038161-3	2012	To shorten beer maturation time, we constructed a self-cloning, bottom-fermenting yeast with low VDK production by integrating ILV5, a gene encoding a protein that metabolizes alpha-acetolactate and alpha-aceto-alpha-hydroxybutyrate (precursors of VDK).	alpha-acetolactate	176-194	ketol-acid reductoisomerase	Saccharomyces cerevisiae S288C	127-131
21370850-1	2011	Acetohydroxy acid synthase (AHAS) is a thiamin diphosphate (ThDP)-dependent enzyme that catalyzes the first common step in the biosynthesis of branched-chain amino acids, condensation of pyruvate with a second 2-ketoacid to form either acetolactate or acetohydroxybutyrate.	alpha-acetolactate	236-248	ilvB acetolactate synthase like	Homo sapiens	0-26
21370850-1	2011	Acetohydroxy acid synthase (AHAS) is a thiamin diphosphate (ThDP)-dependent enzyme that catalyzes the first common step in the biosynthesis of branched-chain amino acids, condensation of pyruvate with a second 2-ketoacid to form either acetolactate or acetohydroxybutyrate.	alpha-acetolactate	236-248	ilvB acetolactate synthase like	Homo sapiens	28-32
18193418-2	2008	On the assumption that part of alpha-acetolactate can be formed also in the cytosol due to a mislocalization of the responsible acetohydroxyacid synthase encoded by ILV2 and ILV6, functional expression in the cytosol of acetohydroxyacid reductoisomerase (Ilv5p) was explored.	alpha-acetolactate	31-49	acetolactate synthase catalytic subunit	Saccharomyces cerevisiae S288C	165-169
18193418-2	2008	On the assumption that part of alpha-acetolactate can be formed also in the cytosol due to a mislocalization of the responsible acetohydroxyacid synthase encoded by ILV2 and ILV6, functional expression in the cytosol of acetohydroxyacid reductoisomerase (Ilv5p) was explored.	alpha-acetolactate	31-49	acetolactate synthase regulatory subunit	Saccharomyces cerevisiae S288C	174-178
18193418-2	2008	On the assumption that part of alpha-acetolactate can be formed also in the cytosol due to a mislocalization of the responsible acetohydroxyacid synthase encoded by ILV2 and ILV6, functional expression in the cytosol of acetohydroxyacid reductoisomerase (Ilv5p) was explored.	alpha-acetolactate	31-49	ketol-acid reductoisomerase	Saccharomyces cerevisiae S288C	255-260
15958189-1	2005	Acetohydroxy acid synthase (AHAS) and related enzymes catalyze the production of chiral compounds [(S)-acetolactate, (S)-acetohydroxybutyrate, or (R)-phenylacetylcarbinol] from achiral substrates (pyruvate, 2-ketobutyrate, or benzaldehyde).	alpha-acetolactate	99-115	ilvB acetolactate synthase like	Homo sapiens	28-32
10986242-14	2000	The purpose of the structure-dependent regulation could be to ensure the minimal production of ALDC required for the control of the acetolactate pool during BCAA synthesis but to avoid its overproduction, which would dissipate acetolactate.	alpha-acetolactate	132-144	aldC	Lactococcus lactis	95-99
10986242-14	2000	The purpose of the structure-dependent regulation could be to ensure the minimal production of ALDC required for the control of the acetolactate pool during BCAA synthesis but to avoid its overproduction, which would dissipate acetolactate.	alpha-acetolactate	227-239	aldC	Lactococcus lactis	95-99