PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
8700867-0	1996	Single-amino acid substitutions eliminate lysine inhibition of maize dihydrodipicolinate synthase.	Lysine	42-48	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	69-97
10608664-1	1999	Dihydrodipicolinate synthase (DHPS) is the main enzyme of a specific branch of the aspartate pathway leading to lysine biosynthesis in higher plants.	Aspartic Acid	83-92	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	30-34
10608664-1	1999	Dihydrodipicolinate synthase (DHPS) is the main enzyme of a specific branch of the aspartate pathway leading to lysine biosynthesis in higher plants.	Lysine	112-118	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	30-34
10608664-3	1999	The DapA open reading frame is interrupted by two introns and encodes the 326 amino acid-long Coix DHPS protein, which is 95% identical to the maize DHPS protein.	2'-deoxyadenylyl-(3'-5')-2'-deoxyadenosine	4-8	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	99-103
10608664-3	1999	The DapA open reading frame is interrupted by two introns and encodes the 326 amino acid-long Coix DHPS protein, which is 95% identical to the maize DHPS protein.	2'-deoxyadenylyl-(3'-5')-2'-deoxyadenosine	4-8	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	149-153
10608664-7	1999	Steady-state levels of DHPS mRNA were slightly reduced in the endosperms and embryos of the maize lysine-rich opaque2 mutants when compared with those in normal kernels.	Lysine	98-104	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	23-27
8700867-1	1996	Dihydrodipicolinate synthase (DHPS; EC 4.2.1.52) catalyzes the first step in biosynthesis of lysine in plants and bacteria.	Lysine	93-99	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	0-28
8700867-1	1996	Dihydrodipicolinate synthase (DHPS; EC 4.2.1.52) catalyzes the first step in biosynthesis of lysine in plants and bacteria.	Lysine	93-99	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	30-34
8700867-2	1996	DHPS in plants is highly sensitive to end-product inhibition by lysine and, therefore, has an important role in regulating metabolite flux into lysine.	Lysine	64-70	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	0-4
8700867-2	1996	DHPS in plants is highly sensitive to end-product inhibition by lysine and, therefore, has an important role in regulating metabolite flux into lysine.	Lysine	144-150	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	0-4
8700867-3	1996	To better understand the feedback inhibition properties of the plant enzyme, we transformed a maize cDNA for lysine-sensitive DHPS into an Escherichia coli strain lacking DHPS activity.	Lysine	109-115	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	126-130
8700867-4	1996	Cells were mutagenized with ethylmethanesulfonate, and potential DHPS mutants were selected by growth on minimal medium containing the inhibitory lysine analogue S-2-aminoethyl-L-cysteine.	Lysine	146-152	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	65-69
8700867-4	1996	Cells were mutagenized with ethylmethanesulfonate, and potential DHPS mutants were selected by growth on minimal medium containing the inhibitory lysine analogue S-2-aminoethyl-L-cysteine.	S-2-aminoethyl cysteine	162-187	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	65-69
8700867-5	1996	DHPS assays identified surviving colonies expressing lysine-insensitive DHPS activity.	Lysine	53-59	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	0-4
8700867-7	1996	No other mutations were present in the remaining DHPS cDNA sequence, indicating that altering only one of the three residues suffices to eliminate lysine inhibition of maize DHPS.	Lysine	147-153	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	174-178
8700867-8	1996	Identification of these specific mutations that change the highly sensitive maize DHPS to a lysine-insensitive isoform will help resolve the lysine-binding mechanism and the resultant conformational changes involved in inhibition of DHPS activity.	Lysine	92-98	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	82-86
8700867-8	1996	Identification of these specific mutations that change the highly sensitive maize DHPS to a lysine-insensitive isoform will help resolve the lysine-binding mechanism and the resultant conformational changes involved in inhibition of DHPS activity.	Lysine	92-98	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	233-237
8700867-8	1996	Identification of these specific mutations that change the highly sensitive maize DHPS to a lysine-insensitive isoform will help resolve the lysine-binding mechanism and the resultant conformational changes involved in inhibition of DHPS activity.	Lysine	141-147	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	82-86
8700867-8	1996	Identification of these specific mutations that change the highly sensitive maize DHPS to a lysine-insensitive isoform will help resolve the lysine-binding mechanism and the resultant conformational changes involved in inhibition of DHPS activity.	Lysine	141-147	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	233-237
8700867-9	1996	The plant-derived mutant DHPS genes may also be used to improve nutritional quality of maize or other cereal grains that have inadequate lysine content when fed to animals such as poultry, swine, or humans.	Lysine	137-143	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	25-29
1886613-1	1991	Dihydrodipicolinate synthase (DHPS; EC 4.2.1.52) is the first committed enzyme in the lysine branch of the aspartate-derived amino acid biosynthesis pathway and is common to bacteria and plants.	Lysine	86-92	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	0-28
24166118-0	1996	Lysine accumulation in maize cell cultures transformed with a lysine-insensitive form of maize dihydrodipicolinate synthase.	Lysine	0-6	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	95-123
24166118-2	1996	Two enzymes in the lysine biosynthesis pathway, aspartate kinase (AK) and dihydrodipicolinate synthase (DHPS), have primary roles in regulating the level of lysine accumulation in plant cells because both enzymes are feedback-inhibited by lysine.	Lysine	19-25	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	74-102
24166118-2	1996	Two enzymes in the lysine biosynthesis pathway, aspartate kinase (AK) and dihydrodipicolinate synthase (DHPS), have primary roles in regulating the level of lysine accumulation in plant cells because both enzymes are feedback-inhibited by lysine.	Lysine	19-25	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	104-108
24166118-2	1996	Two enzymes in the lysine biosynthesis pathway, aspartate kinase (AK) and dihydrodipicolinate synthase (DHPS), have primary roles in regulating the level of lysine accumulation in plant cells because both enzymes are feedback-inhibited by lysine.	Lysine	157-163	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	74-102
24166118-2	1996	Two enzymes in the lysine biosynthesis pathway, aspartate kinase (AK) and dihydrodipicolinate synthase (DHPS), have primary roles in regulating the level of lysine accumulation in plant cells because both enzymes are feedback-inhibited by lysine.	Lysine	157-163	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	104-108
24166118-2	1996	Two enzymes in the lysine biosynthesis pathway, aspartate kinase (AK) and dihydrodipicolinate synthase (DHPS), have primary roles in regulating the level of lysine accumulation in plant cells because both enzymes are feedback-inhibited by lysine.	Lysine	157-163	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	74-102
24166118-2	1996	Two enzymes in the lysine biosynthesis pathway, aspartate kinase (AK) and dihydrodipicolinate synthase (DHPS), have primary roles in regulating the level of lysine accumulation in plant cells because both enzymes are feedback-inhibited by lysine.	Lysine	157-163	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	104-108
24166118-3	1996	An isolated cDNA clone for maize DHPS was modified to encode a DHPS much less sensitive to lysine inhibition.	Lysine	91-97	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	33-37
24166118-3	1996	An isolated cDNA clone for maize DHPS was modified to encode a DHPS much less sensitive to lysine inhibition.	Lysine	91-97	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	63-67
24166118-4	1996	The altered DHPS cDNA was transformed into maize cell suspension cultures to determine the effect on DHPS activity and lysine accumulation.	Lysine	119-125	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	12-16
24166118-5	1996	Partially purified DHPS (wildtype plus mutant) from transformed cultures was less sensitive to lysine inhibition than wild-type DHPS from nontransformed cultures.	Lysine	95-101	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	19-23
24166118-7	1996	Thus, we have shown that reducing the feedback inhibition of DHPS by lysine can lead to increased lysine accumulation in maize cells.	Lysine	69-75	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	61-65
24166118-7	1996	Thus, we have shown that reducing the feedback inhibition of DHPS by lysine can lead to increased lysine accumulation in maize cells.	Lysine	98-104	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	61-65
1886613-1	1991	Dihydrodipicolinate synthase (DHPS; EC 4.2.1.52) is the first committed enzyme in the lysine branch of the aspartate-derived amino acid biosynthesis pathway and is common to bacteria and plants.	Lysine	86-92	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	30-34
1886613-1	1991	Dihydrodipicolinate synthase (DHPS; EC 4.2.1.52) is the first committed enzyme in the lysine branch of the aspartate-derived amino acid biosynthesis pathway and is common to bacteria and plants.	Aspartic Acid	107-116	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	0-28
1886613-1	1991	Dihydrodipicolinate synthase (DHPS; EC 4.2.1.52) is the first committed enzyme in the lysine branch of the aspartate-derived amino acid biosynthesis pathway and is common to bacteria and plants.	Aspartic Acid	107-116	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	30-34
1886613-2	1991	Due to feedback inhibition by lysine, DHPS serves in a regulatory role for this pathway in plant metabolism.	Lysine	30-36	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	38-42
1886613-3	1991	To elucidate the molecular genetic characteristics of DHPS, we isolated a putative full-length cDNA clone for maize DHPS by direct genetic selection in an Escherichia coli dapA- auxotroph.	2'-deoxyadenylyl-(3'-5')-2'-deoxyadenosine	172-176	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	116-120
1886613-4	1991	The maize DHPS activity expressed in the complemented E. coli auxotroph showed the lysine inhibition characteristics of purified maize DHPS, indicating that the cDNA encoded sequences for both the catalytic function and regulatory properties of the enzyme.	Lysine	83-89	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	10-14
1886613-4	1991	The maize DHPS activity expressed in the complemented E. coli auxotroph showed the lysine inhibition characteristics of purified maize DHPS, indicating that the cDNA encoded sequences for both the catalytic function and regulatory properties of the enzyme.	Lysine	83-89	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	135-139
16668206-1	1991	Dihydrodipicolinate synthase (EC 4.2.1.52), the first enzyme specific to lysine biosynthesis in plants, was purified from maize (Zea mays L.) cell suspension cultures and leaves.	Lysine	73-79	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	0-28
16668206-2	1991	The subunit molecular weight of maize dihydrodipicolinate synthase was estimated to be 38,000 based on SDS-PAGE.	Sodium Dodecyl Sulfate	103-106	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	38-66
16668206-3	1991	The condensation of l-aspartate semialdehyde and pyruvate by highly purified dihydrodipicolinate synthase exhibited kinetics characteristic of a Ping Pong Bi Bi ordered reaction in which pyruvate binds first to the enzyme.	Pyruvic Acid	49-57	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	77-105
16668206-3	1991	The condensation of l-aspartate semialdehyde and pyruvate by highly purified dihydrodipicolinate synthase exhibited kinetics characteristic of a Ping Pong Bi Bi ordered reaction in which pyruvate binds first to the enzyme.	Pyruvic Acid	187-195	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	77-105
16668206-7	1991	Lysine was an allosteric cooperative inhibitor of dihydrodipicolinate synthase with an estimated Hill number of 4 and 23 micromolar concentration required for 50% inhibition.	Lysine	0-6	4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic	Zea mays	50-78