PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
9022075-0	1997	Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanal, and acrolein.	lactaldehyde	131-148	myeloperoxidase	Homo sapiens	29-44
18439018-9	2008	2-Methylfuran was preferably formed in the presence of amino acids by aldol-type reactions of C(2) and C(3) fragments with lactaldehyde as a key intermediate, the Strecker aldehyde of threonine.	lactaldehyde	123-135	complement C2	Homo sapiens	94-98
12921788-1	2003	Activated phagocytes employ myeloperoxidase to generate glycolaldehyde, 2-hydroxypropanal, and acrolein.	lactaldehyde	72-89	myeloperoxidase	Homo sapiens	28-43
2644239-5	1989	Anaerobically, lactaldehyde is reduced to L-1,2-propanediol by an NADH-linked oxidoreductase (fucO product).	lactaldehyde	15-27	oxidoreductase	Escherichia coli	78-92
1730033-1	1992	1,2-Propanediol oxidoreductase, which reduces the L-lactaldehyde formed in the fermentation of L-fucose or L-rhamnose to L-1,2-propanediol in E. coli, was inactivated by a component of E. coli cell extracts in the presence of oxygen.	lactaldehyde	50-64	oxidoreductase	Escherichia coli	16-30
8974076-2	1996	The results indicate that D, and L-lactaldehyde are strong non-competitive inhibitors of glyoxalase I and the effect with the D-isomer is more pronounced, whereas both D,L-glyceraldehyde and acetaldehyde are moderately inhibitory and the nature of inhibition is strictly competitive.	lactaldehyde	33-47	glyoxalase 1	Mus musculus	89-101
1684935-2	1991	In Escherichia coli, an aldehyde dehydrogenase that catalyzes the oxidation of L-lactaldehyde to L-lactate is induced not only by L-fucose, L-rhamnose or D-arabinose, but also by growth in the presence of glutamate or amino acids yielding glutamate, with the exception of proline.	lactaldehyde	79-93	Aldehyde dehydrogenase	Escherichia coli	24-46
2644239-7	1989	In a previous study, we showed that retention of the C-4-to-C-6 fragment of fucose depended on the competition for lactaldehyde by aldehyde dehydrogenase and propanediol oxidoreductase (Y. Zhu and E.C.C.	lactaldehyde	115-127	oxidoreductase	Escherichia coli	170-184
3298215-1	1987	Mutant analysis revealed that complete utilization of L-fucose and L-rhamnose by Escherichia coli requires the activity of a common NAD-linked aldehyde dehydrogenase which converts L-lactaldehyde to L-lactate.	lactaldehyde	181-195	Aldehyde dehydrogenase	Escherichia coli	143-165
3904730-2	1985	The enzyme propanediol oxidoreductase, which converts the lactaldehyde formed in the metabolism of fucose and rhamnose into propane-1,2-diol under anaerobic conditions, was investigated in Escherichia coli, Klebsiella pneumoniae and Salmonella typhimurium.	lactaldehyde	58-70	oxidoreductase	Escherichia coli	23-37
3542971-2	1987	Aerobically, L-lactaldehyde serves as a carbon and energy source by the action of an aldehyde dehydrogenase of broad specificity; the product, L-lactate, is then converted to pyruvate.	lactaldehyde	13-27	Aldehyde dehydrogenase	Escherichia coli	85-107
3542971-3	1987	Anaerobically, L-lactaldehyde serves as an electron acceptor to regenerate NAD from NADH by the action of an oxidoreductase; the reduced product, L-12-propanediol, is excreted.	lactaldehyde	15-29	oxidoreductase	Escherichia coli	109-123
3542971-12	1987	Complete aerobic utilization of carbons 4 through 6 of L-fucose depends not only on an adequate activity of aldehyde dehydrogenase to trap L-lactaldehyde as its anionic acid but also on the lack of L-1,2-propanediol oxidoreductase activity, which converts L-lactaldehyde to a readily excreted alcohol.	lactaldehyde	139-153	Aldehyde dehydrogenase	Escherichia coli	108-130
3542971-12	1987	Complete aerobic utilization of carbons 4 through 6 of L-fucose depends not only on an adequate activity of aldehyde dehydrogenase to trap L-lactaldehyde as its anionic acid but also on the lack of L-1,2-propanediol oxidoreductase activity, which converts L-lactaldehyde to a readily excreted alcohol.	lactaldehyde	256-270	Aldehyde dehydrogenase	Escherichia coli	108-130
6427403-3	1984	From the deleted strain we derived a constitutive producer of propanediol oxidoreductase able to grow on 1,2-propanediol by oxidizing the diol to lactaldehyde which was further metabolized to lactate.	lactaldehyde	146-158	oxidoreductase	Escherichia coli	74-88
361712-3	1978	These strains synthesize at high constitutive levels a propanediolmicotinamide adenine dinucleotide oxidoreductase, an enzyme serving as a lactaldehyde during L-fucose fermentation by wild type cells.	lactaldehyde	139-151	oxidoreductase	Escherichia coli	100-114
30822216-3	2019	Lactaldehyde (LA) is formed from a reaction between threonine and myeloperoxidase, but no LA-derived AGEs have been characterized.	lactaldehyde	0-12	myeloperoxidase	Rattus norvegicus	66-81
853309-0	1977	Assay of brain and liver alcohol dehydrogenase by the coupled oxido-reduction of ethanol and lactaldehyde in the presence of deoxycholate.	lactaldehyde	93-105	aldo-keto reductase family 1 member A1	Homo sapiens	25-46
33204871-3	2020	Here, we report a novel crosslinked type of AGE, named as lactaldehyde-derived lysine dimer (LAK2), which is produced due to non-enzymatic glycation of N alpha-acetyl-L-lysine with lactaldehyde under physiological conditions.	lactaldehyde	58-70	renin binding protein	Homo sapiens	44-47
33204871-3	2020	Here, we report a novel crosslinked type of AGE, named as lactaldehyde-derived lysine dimer (LAK2), which is produced due to non-enzymatic glycation of N alpha-acetyl-L-lysine with lactaldehyde under physiological conditions.	lactaldehyde	181-193	renin binding protein	Homo sapiens	44-47
33204871-6	2020	Since lactaldehyde is known to be produced from L-threonine in a myeloperoxidase (MPO)-mediated reaction at sites of inflammation, LAK2 has the potential to be an oxidative stress marker of MPO-mediated reactions induced in inflammation.	lactaldehyde	6-18	myeloperoxidase	Homo sapiens	65-80
33204871-6	2020	Since lactaldehyde is known to be produced from L-threonine in a myeloperoxidase (MPO)-mediated reaction at sites of inflammation, LAK2 has the potential to be an oxidative stress marker of MPO-mediated reactions induced in inflammation.	lactaldehyde	6-18	myeloperoxidase	Homo sapiens	82-85
33204871-6	2020	Since lactaldehyde is known to be produced from L-threonine in a myeloperoxidase (MPO)-mediated reaction at sites of inflammation, LAK2 has the potential to be an oxidative stress marker of MPO-mediated reactions induced in inflammation.	lactaldehyde	6-18	myeloperoxidase	Homo sapiens	190-193