PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
7483670-0	1995	Aminium cation radical mechanism proposed for monoamine oxidase B catalysis: are there alternatives?	aminium	0-7	monoamine oxidase B	Bos taurus	46-65
8937512-2	1996	In the present study, the effect of an antiparkinsonian agent, deprenyl (selegeline hydrochloride) which is believed to be a selective inhibitor of monoamine oxidase-B, on bovine brain calmodulin-dependent cyclic nucleotide phosphodiesterase (CaMPDE) isozymes have been investigated.	Selegiline	63-71	monoamine oxidase B	Bos taurus	148-167
8937512-2	1996	In the present study, the effect of an antiparkinsonian agent, deprenyl (selegeline hydrochloride) which is believed to be a selective inhibitor of monoamine oxidase-B, on bovine brain calmodulin-dependent cyclic nucleotide phosphodiesterase (CaMPDE) isozymes have been investigated.	selegeline hydrochloride	73-97	monoamine oxidase B	Bos taurus	148-167
7483670-2	1995	The interaction of bovine liver mitochondrial monoamine oxidase B (MAO B) with a series of benzylamine analogues was investigated to provide mechanistic information relative to the proposed cation radical mechanism and to provide information on the structural requirements of the substrate binding site.	benzylamine	91-102	monoamine oxidase B	Bos taurus	46-65
7483670-2	1995	The interaction of bovine liver mitochondrial monoamine oxidase B (MAO B) with a series of benzylamine analogues was investigated to provide mechanistic information relative to the proposed cation radical mechanism and to provide information on the structural requirements of the substrate binding site.	benzylamine	91-102	monoamine oxidase B	Bos taurus	67-72
7483670-4	1995	Steady-state kinetic analysis of MAO B with 11 ring-substituted benzylamine analogues showed substitution does not alter the reaction pathway.	benzylamine	64-75	monoamine oxidase B	Bos taurus	33-38
7483670-9	1995	The binding affinity of para-substituted benzylamine analogues to MAO B increased as the hydrophobicity of the substituent increased.	benzylamine	41-52	monoamine oxidase B	Bos taurus	66-71
7483670-15	1995	In contrast, meta-substituted N,N-dimethyl benzylamine analogues are weak substrates for MAO B with oxidation occurring exclusively at the benzyl carbon.	N-benzyl-N,N-dimethylamine	30-54	monoamine oxidase B	Bos taurus	89-94
7483670-15	1995	In contrast, meta-substituted N,N-dimethyl benzylamine analogues are weak substrates for MAO B with oxidation occurring exclusively at the benzyl carbon.	Carbon	146-152	monoamine oxidase B	Bos taurus	89-94
7483670-17	1995	The consequences of these results on the possible mechanisms (aminium cation radical, H abstraction, and nucleophilic mechanism) for C-H bond cleavage proposed for MAO B are discussed.	aminium cation radical	62-84	monoamine oxidase B	Bos taurus	164-169
7483670-17	1995	The consequences of these results on the possible mechanisms (aminium cation radical, H abstraction, and nucleophilic mechanism) for C-H bond cleavage proposed for MAO B are discussed.	Carbon	133-134	monoamine oxidase B	Bos taurus	164-169
7699568-9	1994	In contrast, all the beta-carbolines investigated in this study had low potencies as inhibitors of monoamine oxidase B.	Carbolines	21-36	monoamine oxidase B	Bos taurus	99-118
8589074-1	1995	The influence of para and meta substitution of benzylamine analogues on their interaction with bovine liver monoamine oxidase B has been investigated to provide insights into the nature of the substrate binding site.	benzylamine	47-58	monoamine oxidase B	Bos taurus	108-127
7931239-0	1994	Acetylenic and allenic derivatives of 2-(5-methoxy-1-methylindolyl)alkylamines as selective inhibitors of MAO-A and MAO-B.	2-(5-methoxy-1-methylindolyl)alkylamines	38-78	monoamine oxidase B	Bos taurus	116-121
8003474-0	1994	Structure-activity relationships in the oxidation of benzylamine analogues by bovine liver mitochondrial monoamine oxidase B.	benzylamine	53-64	monoamine oxidase B	Bos taurus	105-124
8003474-1	1994	The influence of para and meta substitution of benzylamine on its interaction with bovine liver mitochondrial monoamine oxidase B (MAO B) has been investigated by steady-state and reductive half-reaction anaerobic stopped-flow kinetic approaches.	benzylamine	47-58	monoamine oxidase B	Bos taurus	110-129
8003474-1	1994	The influence of para and meta substitution of benzylamine on its interaction with bovine liver mitochondrial monoamine oxidase B (MAO B) has been investigated by steady-state and reductive half-reaction anaerobic stopped-flow kinetic approaches.	benzylamine	47-58	monoamine oxidase B	Bos taurus	131-136
8003474-16	1994	para-Substituted benzylamine analogues reduce MAO B with limiting rates that correlate with the steric influence (Es value) of the substituent.	benzylamine	17-28	monoamine oxidase B	Bos taurus	46-51
8003474-17	1994	Statistical analysis shows the rate of MAO B reduction by para-substituted analogues to be retarded by increased values of Es and, with a smaller contribution, by the hydrophobicity value of the substituent.	Einsteinium	123-125	monoamine oxidase B	Bos taurus	39-44
8003474-18	1994	The rate of MAO B reduction by meta-substituted benzylamine analogues is essentially independent of the nature of the substituent.	benzylamine	48-59	monoamine oxidase B	Bos taurus	12-17
8003474-20	1994	These data demonstrate the steric orientation of the substrate to be important in the rate of amine oxidation by MAO B and that ring meta substituents favor this orientation.	Amines	94-99	monoamine oxidase B	Bos taurus	113-118
7931239-1	1994	A new series of thirty derivatives of 2-(5-methoxy-1-methylindolyl)alkylamines has been synthesized and the compounds assayed as inhibitors of MAO-A and MAO-B from bovine brain mitochondria.	2-(5-methoxy-1-methylindolyl)alkylamines	38-78	monoamine oxidase B	Bos taurus	153-158
1797336-3	1991	In vitro and in vivo studies, with numerous tissues, including adrenal chromaffin cells, have clearly shown that the formation of the latter metabolites is exclusively mediated by monoamine oxidase B for which milacemide is a substrate.	chromaffin	71-81	monoamine oxidase B	Bos taurus	180-199
8494896-0	1993	Spectral and kinetic studies of imine product formation in the oxidation of p-(N,N-dimethylamino)benzylamine analogues by monoamine oxidase B.	Imines	32-37	monoamine oxidase B	Bos taurus	122-141
8494896-0	1993	Spectral and kinetic studies of imine product formation in the oxidation of p-(N,N-dimethylamino)benzylamine analogues by monoamine oxidase B.	p-(n,n-dimethylamino)benzylamine	76-108	monoamine oxidase B	Bos taurus	122-141
8494896-1	1993	The oxidative deamination of p-(N,N-dimethylamino)benzylamine and N-methyl-p-(N,N-dimethylamino)benzylamine by bovine liver monoamine oxidase B has been investigated by absorption spectral, steady-state, and stopped-flow kinetic studies.	p-(n,n-dimethylamino)benzylamine	29-61	monoamine oxidase B	Bos taurus	124-143
8494896-1	1993	The oxidative deamination of p-(N,N-dimethylamino)benzylamine and N-methyl-p-(N,N-dimethylamino)benzylamine by bovine liver monoamine oxidase B has been investigated by absorption spectral, steady-state, and stopped-flow kinetic studies.	n-methyl-p-(n,n-dimethylamino)benzylamine	66-107	monoamine oxidase B	Bos taurus	124-143
8424650-1	1993	The flavoprotein monoamine oxidase B (MAO B) from bovine liver, as isolated, has an unusual additional absorption band at 412 nm, which is similar to the absorption of its anionic flavin semiquinone form, (Fl.-), and other typical (Fl.-) flavoproteins.	flavin semiquinone	180-198	monoamine oxidase B	Bos taurus	17-36
8424650-1	1993	The flavoprotein monoamine oxidase B (MAO B) from bovine liver, as isolated, has an unusual additional absorption band at 412 nm, which is similar to the absorption of its anionic flavin semiquinone form, (Fl.-), and other typical (Fl.-) flavoproteins.	flavin semiquinone	180-198	monoamine oxidase B	Bos taurus	38-43
8424650-3	1993	The resonance Raman (RR) spectrum of MAO B as isolated is virtually identical to that of its dithionite-reduced (Fl.-) form.	Dithionite	93-103	monoamine oxidase B	Bos taurus	37-42
1540641-5	1992	We have now found that although this aldehyde inhibits MAO B competitively (Ki 0.017 mM) this cannot account for the inhibitory process, since during a 60 min incubation with the substrate (0.5 mM; Km, 0.074 mM) more than 95% inhibition of MAO B was observed and the concentration of aldehyde had reached approx.	Aldehydes	37-45	monoamine oxidase B	Bos taurus	55-60
1540641-5	1992	We have now found that although this aldehyde inhibits MAO B competitively (Ki 0.017 mM) this cannot account for the inhibitory process, since during a 60 min incubation with the substrate (0.5 mM; Km, 0.074 mM) more than 95% inhibition of MAO B was observed and the concentration of aldehyde had reached approx.	Aldehydes	37-45	monoamine oxidase B	Bos taurus	240-245
1540641-5	1992	We have now found that although this aldehyde inhibits MAO B competitively (Ki 0.017 mM) this cannot account for the inhibitory process, since during a 60 min incubation with the substrate (0.5 mM; Km, 0.074 mM) more than 95% inhibition of MAO B was observed and the concentration of aldehyde had reached approx.	Aldehydes	284-292	monoamine oxidase B	Bos taurus	55-60
1540641-9	1992	Oxidation of N-methyl-E-cinnamylamine and its Z-isomer by MAO B produced progress curves similar to that obtained with the primary amine, but in these cases inhibition was not reversed either by dilution or dialysis.	n-methyl-e-cinnamylamine	13-37	monoamine oxidase B	Bos taurus	58-63
1540641-9	1992	Oxidation of N-methyl-E-cinnamylamine and its Z-isomer by MAO B produced progress curves similar to that obtained with the primary amine, but in these cases inhibition was not reversed either by dilution or dialysis.	Amines	32-37	monoamine oxidase B	Bos taurus	58-63
1540641-10	1992	Partition ratios for the pair of N-methyl isomers with bovine MAO B were calculated to be 1640 (E-isomer) and 1430 (Z-isomer).	Nitrogen	33-34	monoamine oxidase B	Bos taurus	62-67
1540641-12	1992	A tritiated form of N-methyl-E-cinnamylamine, incubated with MAO B from bovine liver, resulted in incorporation of radioactivity into the enzyme.	n-methyl-e-cinnamylamine	20-44	monoamine oxidase B	Bos taurus	61-66
1797336-3	1991	In vitro and in vivo studies, with numerous tissues, including adrenal chromaffin cells, have clearly shown that the formation of the latter metabolites is exclusively mediated by monoamine oxidase B for which milacemide is a substrate.	milacemide	210-220	monoamine oxidase B	Bos taurus	180-199
1797336-11	1991	The release of catecholamines from chromaffin cells in response to milacemide (10(-4) M) was partially inhibited by the selective MAO-B inhibitors (-)-deprenyl (10(-7) M) and AGN 1135 (10(-6) M).	Catecholamines	15-29	monoamine oxidase B	Bos taurus	130-135
1797336-11	1991	The release of catecholamines from chromaffin cells in response to milacemide (10(-4) M) was partially inhibited by the selective MAO-B inhibitors (-)-deprenyl (10(-7) M) and AGN 1135 (10(-6) M).	chromaffin	35-45	monoamine oxidase B	Bos taurus	130-135
1797336-11	1991	The release of catecholamines from chromaffin cells in response to milacemide (10(-4) M) was partially inhibited by the selective MAO-B inhibitors (-)-deprenyl (10(-7) M) and AGN 1135 (10(-6) M).	milacemide	67-77	monoamine oxidase B	Bos taurus	130-135
1797336-11	1991	The release of catecholamines from chromaffin cells in response to milacemide (10(-4) M) was partially inhibited by the selective MAO-B inhibitors (-)-deprenyl (10(-7) M) and AGN 1135 (10(-6) M).	Selegiline	147-159	monoamine oxidase B	Bos taurus	130-135
1797336-11	1991	The release of catecholamines from chromaffin cells in response to milacemide (10(-4) M) was partially inhibited by the selective MAO-B inhibitors (-)-deprenyl (10(-7) M) and AGN 1135 (10(-6) M).	rasagiline	175-183	monoamine oxidase B	Bos taurus	130-135
1797336-12	1991	This indicates that the MAO-B derived metabolites, glycineamide and glycine, contribute to the secretion of catecholamines as does milacemide itself.	glycine amide	51-63	monoamine oxidase B	Bos taurus	24-29
1797336-12	1991	This indicates that the MAO-B derived metabolites, glycineamide and glycine, contribute to the secretion of catecholamines as does milacemide itself.	Glycine	51-58	monoamine oxidase B	Bos taurus	24-29
1797336-12	1991	This indicates that the MAO-B derived metabolites, glycineamide and glycine, contribute to the secretion of catecholamines as does milacemide itself.	Catecholamines	108-122	monoamine oxidase B	Bos taurus	24-29
1797336-12	1991	This indicates that the MAO-B derived metabolites, glycineamide and glycine, contribute to the secretion of catecholamines as does milacemide itself.	milacemide	131-141	monoamine oxidase B	Bos taurus	24-29
2323731-6	1990	In contrast, only a slight reduction was observed with deprenyl as MAO B inhibitor.	Selegiline	55-63	monoamine oxidase B	Bos taurus	67-72
1972391-4	1990	The addition of an inhibitor of monoamine oxidase (MAO) B (Ro 19-6327), but not MAO A (clorgyline), prevented the toxicity of MPTP but not that of MPP+.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	126-130	monoamine oxidase B	Bos taurus	32-57
3137478-2	1988	1) Exposure to (-)-deprenyl, an irreversible inhibitor of monoamine oxidase B, markedly potentiated the contractions caused by tryptamine but not those by 5-hydroxy-tryptamine (5-HT).	Selegiline	15-27	monoamine oxidase B	Bos taurus	58-77
2128507-4	1990	The kinetic constants towards benzylamine showed SSAO to have a higher affinity than MAO-B, and the comparison of the Vmax/Km relationship for both enzymes indicated that benzylamine would be oxidised more efficiently by SSAO than by MAO-B.	benzylamine	30-41	monoamine oxidase B	Bos taurus	85-90
2128507-4	1990	The kinetic constants towards benzylamine showed SSAO to have a higher affinity than MAO-B, and the comparison of the Vmax/Km relationship for both enzymes indicated that benzylamine would be oxidised more efficiently by SSAO than by MAO-B.	benzylamine	30-41	monoamine oxidase B	Bos taurus	234-239
2128507-4	1990	The kinetic constants towards benzylamine showed SSAO to have a higher affinity than MAO-B, and the comparison of the Vmax/Km relationship for both enzymes indicated that benzylamine would be oxidised more efficiently by SSAO than by MAO-B.	benzylamine	171-182	monoamine oxidase B	Bos taurus	85-90
2128507-4	1990	The kinetic constants towards benzylamine showed SSAO to have a higher affinity than MAO-B, and the comparison of the Vmax/Km relationship for both enzymes indicated that benzylamine would be oxidised more efficiently by SSAO than by MAO-B.	benzylamine	171-182	monoamine oxidase B	Bos taurus	234-239
2458966-3	1988	ATP is not required for the binding of the newly synthesized enzyme to the outer membranes, but is necessary for the insertion of MAO B into these membrane vesicles.	Adenosine Triphosphate	0-3	monoamine oxidase B	Bos taurus	130-135
2838087-1	1988	The spin-labeled substrate, tryptamine, was used as a structural probe of the active site of bovine liver monoamine oxidase B (amine:oxygen oxidoreductase (deaminating) (flavin-containing), EC 1.4.3.4).	tryptamine	28-38	monoamine oxidase B	Bos taurus	106-125
2838087-1	1988	The spin-labeled substrate, tryptamine, was used as a structural probe of the active site of bovine liver monoamine oxidase B (amine:oxygen oxidoreductase (deaminating) (flavin-containing), EC 1.4.3.4).	4,6-dinitro-o-cresol	170-176	monoamine oxidase B	Bos taurus	106-125
3137478-2	1988	1) Exposure to (-)-deprenyl, an irreversible inhibitor of monoamine oxidase B, markedly potentiated the contractions caused by tryptamine but not those by 5-hydroxy-tryptamine (5-HT).	tryptamine	127-137	monoamine oxidase B	Bos taurus	58-77
3496919-0	1987	Stopped-flow studies on the mechanism of oxidation of N-methyl-4-phenyltetrahydropyridine by bovine liver monoamine oxidase B.	n-methyl-4-phenyltetrahydropyridine	54-89	monoamine oxidase B	Bos taurus	106-125
3592682-1	1987	The reaction of 2-chloro-2-phenylethylamine with monoamine oxidase B was investigated to study the mechanism of this enzyme and its inactivation by this compound.	2-Chloro-2-phenylethanamine	16-43	monoamine oxidase B	Bos taurus	49-68
3592682-4	1987	During the mechanistic studies we noted time-dependent inactivation of monoamine oxidase B by 2-chloro-2-phenylethylamine under both aerobic and anaerobic conditions.	2-Chloro-2-phenylethanamine	94-121	monoamine oxidase B	Bos taurus	71-90
3592682-8	1987	Anaerobic reaction of 2-chloro-2-phenylethylamine with monoamine oxidase B probably proceeds by direct alkylation of an enzyme residue (tau 1/2 = 140 min).	2-Chloro-2-phenylethanamine	22-49	monoamine oxidase B	Bos taurus	55-74
6549266-3	1984	In a far lesser degree these preparations inhibited the deamination of benzylamine, a specific substrate for monoamine oxidase B.	benzylamine	71-82	monoamine oxidase B	Bos taurus	109-128
3928814-7	1985	In other experiments, MPTP was an excellent substrate for pure MAO-B, prepared from bovine liver.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	22-26	monoamine oxidase B	Bos taurus	63-68
6424235-2	1984	This monoamine oxidase B enzyme was somewhat distinct from B enzymes from other sources, in that noradrenaline was a much poorer substrate than serotonin.	Norepinephrine	97-110	monoamine oxidase B	Bos taurus	5-24
6424235-2	1984	This monoamine oxidase B enzyme was somewhat distinct from B enzymes from other sources, in that noradrenaline was a much poorer substrate than serotonin.	Serotonin	144-153	monoamine oxidase B	Bos taurus	5-24
17447421-2	2006	Hydroxyzine was found to be a competitive inhibitor of MAO-B (Ki - 38 microM), whereas it had a low potency towards MAO-A (IC50 > 630 microM).	Hydroxyzine	0-11	monoamine oxidase B	Bos taurus	55-60
685198-0	1978	[Monoamine oxidation in the mitochondrial fraction of bovine kidney catalyzed by monoamine oxidase type B].	monoamine	1-10	monoamine oxidase B	Bos taurus	81-105
18799315-0	2008	Deuterium isotope effects for the oxidation of 1-methyl-3-phenyl-3-pyrrolinyl analogues by monoamine oxidase B.	Deuterium	0-9	monoamine oxidase B	Bos taurus	91-110
18799315-0	2008	Deuterium isotope effects for the oxidation of 1-methyl-3-phenyl-3-pyrrolinyl analogues by monoamine oxidase B.	1-methyl-3-phenyl-3-pyrrolinyl	47-77	monoamine oxidase B	Bos taurus	91-110
18799315-1	2008	The parkinsonian inducing agent, 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), is a cyclic tertiary allylamine exhibiting good monoamine oxidase B (MAO-B) substrate properties.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	33-77	monoamine oxidase B	Bos taurus	134-153
18799315-1	2008	The parkinsonian inducing agent, 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), is a cyclic tertiary allylamine exhibiting good monoamine oxidase B (MAO-B) substrate properties.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	33-77	monoamine oxidase B	Bos taurus	155-160
18799315-1	2008	The parkinsonian inducing agent, 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), is a cyclic tertiary allylamine exhibiting good monoamine oxidase B (MAO-B) substrate properties.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	79-83	monoamine oxidase B	Bos taurus	134-153
18799315-1	2008	The parkinsonian inducing agent, 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), is a cyclic tertiary allylamine exhibiting good monoamine oxidase B (MAO-B) substrate properties.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	79-83	monoamine oxidase B	Bos taurus	155-160
18799315-1	2008	The parkinsonian inducing agent, 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), is a cyclic tertiary allylamine exhibiting good monoamine oxidase B (MAO-B) substrate properties.	Allylamine	107-117	monoamine oxidase B	Bos taurus	134-153
18799315-1	2008	The parkinsonian inducing agent, 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), is a cyclic tertiary allylamine exhibiting good monoamine oxidase B (MAO-B) substrate properties.	Allylamine	107-117	monoamine oxidase B	Bos taurus	155-160
18799315-2	2008	MAO-B catalyzes the ring alpha-carbon 2-electron bioactivation of MPTP to yield the 1-methyl-4-phenyl-2,3-dihydropyridinium species (MPDP(+)).	Carbon	31-37	monoamine oxidase B	Bos taurus	0-5
18799315-2	2008	MAO-B catalyzes the ring alpha-carbon 2-electron bioactivation of MPTP to yield the 1-methyl-4-phenyl-2,3-dihydropyridinium species (MPDP(+)).	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	66-70	monoamine oxidase B	Bos taurus	0-5
18799315-2	2008	MAO-B catalyzes the ring alpha-carbon 2-electron bioactivation of MPTP to yield the 1-methyl-4-phenyl-2,3-dihydropyridinium species (MPDP(+)).	1-methyl-4-phenyl-2,3-dihydropyridinium	84-123	monoamine oxidase B	Bos taurus	0-5
18799315-3	2008	The corresponding 5-membered ring MPTP analogue, 1-methyl-3-phenyl-3-pyrroline, also undergoes MAO-B-catalyzed oxidation to give the 2-electron oxidation product, 1-methyl-3-phenylpyrrole.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	34-38	monoamine oxidase B	Bos taurus	95-100
18799315-3	2008	The corresponding 5-membered ring MPTP analogue, 1-methyl-3-phenyl-3-pyrroline, also undergoes MAO-B-catalyzed oxidation to give the 2-electron oxidation product, 1-methyl-3-phenylpyrrole.	1-methyl-3-phenyl-3-pyrroline	49-78	monoamine oxidase B	Bos taurus	95-100
18799315-3	2008	The corresponding 5-membered ring MPTP analogue, 1-methyl-3-phenyl-3-pyrroline, also undergoes MAO-B-catalyzed oxidation to give the 2-electron oxidation product, 1-methyl-3-phenylpyrrole.	1-methyl-3-phenyl-1H-pyrrole	163-187	monoamine oxidase B	Bos taurus	95-100
18799315-6	2008	The values reported for the oxidation of MPTP by bovine liver MAO-B with MPTP-6,6-d(2), as deuterated substrate, are (D)(V(max))=3.55; (D)(V(max)/K(m))=8.01.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	41-45	monoamine oxidase B	Bos taurus	62-67
18799315-6	2008	The values reported for the oxidation of MPTP by bovine liver MAO-B with MPTP-6,6-d(2), as deuterated substrate, are (D)(V(max))=3.55; (D)(V(max)/K(m))=8.01.	mptp-6,6-d	73-83	monoamine oxidase B	Bos taurus	62-67
18799315-7	2008	We conclude that the mechanism of the MAO-B-catalyzed oxidation of pyrrolinyl substrates is similar to that of the tetrahydropyridinyl substrates and that a carbon-hydrogen bond cleavage step is, at least partially, rate determining.	Carbon	157-163	monoamine oxidase B	Bos taurus	38-43
18799315-7	2008	We conclude that the mechanism of the MAO-B-catalyzed oxidation of pyrrolinyl substrates is similar to that of the tetrahydropyridinyl substrates and that a carbon-hydrogen bond cleavage step is, at least partially, rate determining.	Hydrogen	164-172	monoamine oxidase B	Bos taurus	38-43
15710600-6	2005	Ile-199 is conserved in all known MAO B sequences except bovine MAO B, which has Phe in this position (the sequence of sheep MAO B is unknown).	Isoleucine	0-3	monoamine oxidase B	Bos taurus	34-39
15710600-6	2005	Ile-199 is conserved in all known MAO B sequences except bovine MAO B, which has Phe in this position (the sequence of sheep MAO B is unknown).	Isoleucine	0-3	monoamine oxidase B	Bos taurus	64-69
15710600-6	2005	Ile-199 is conserved in all known MAO B sequences except bovine MAO B, which has Phe in this position (the sequence of sheep MAO B is unknown).	Phenylalanine	81-84	monoamine oxidase B	Bos taurus	64-69
11425554-0	2001	Inactivation of monoamine oxidase B by 1-phenylcyclopropylamine: mass spectral evidence for the flavin adduct.	1-phenylcyclopropylamine	39-63	monoamine oxidase B	Bos taurus	16-35
11425554-0	2001	Inactivation of monoamine oxidase B by 1-phenylcyclopropylamine: mass spectral evidence for the flavin adduct.	4,6-dinitro-o-cresol	96-102	monoamine oxidase B	Bos taurus	16-35
11425554-1	2001	Incubation of 1-phenylcyclopropylamine with bovine liver MAO (MAO B), followed by complete enzymatic digestion to single amino acid residues and subsequent analysis by on-line liquid chromatography-electrospray ionization mass spectrometry, was used to investigate the resulting flavin adduct structure.	1-phenylcyclopropylamine	14-38	monoamine oxidase B	Bos taurus	62-67
11004529-0	2000	Evidence for alternative binding modes in the interaction of benzylamine analogues with bovine liver monoamine oxidase B.	benzylamine	61-72	monoamine oxidase B	Bos taurus	101-120
11004529-1	2000	The interaction of purified bovine liver MAO B with the benzylamine analogues N,N-dimethylbenzylamine and alpha-methylbenzylamine has been investigated.	benzylamine	56-67	monoamine oxidase B	Bos taurus	41-46
11004529-1	2000	The interaction of purified bovine liver MAO B with the benzylamine analogues N,N-dimethylbenzylamine and alpha-methylbenzylamine has been investigated.	N-benzyl-N,N-dimethylamine	78-101	monoamine oxidase B	Bos taurus	41-46
11004529-1	2000	The interaction of purified bovine liver MAO B with the benzylamine analogues N,N-dimethylbenzylamine and alpha-methylbenzylamine has been investigated.	1-phenethylamine	106-129	monoamine oxidase B	Bos taurus	41-46
11004529-4	2000	Analysis of the binding affinities demonstrate the deprotonated forms of the tertiary amines are preferentially bound to MAO B and the affinity decreases with increasing van der Waals volume of the para-substituent.	Amines	86-92	monoamine oxidase B	Bos taurus	121-126
11004529-6	2000	75+/-0.11)(0.1xV(w))-4.24+/-(0.16)alpha-Methyl benzylamine analogues are also found to be competitive inhibitors of MAO B-catalyzed benzylamine oxidation.	1-phenethylamine	34-58	monoamine oxidase B	Bos taurus	116-121
11004529-6	2000	75+/-0.11)(0.1xV(w))-4.24+/-(0.16)alpha-Methyl benzylamine analogues are also found to be competitive inhibitors of MAO B-catalyzed benzylamine oxidation.	benzylamine	47-58	monoamine oxidase B	Bos taurus	116-121
11004529-8	2000	Analysis of the binding affinities of five para-substituted alpha-methylbenzylamine analogues to MAO B shows the deprotonated form also to be preferentially bound and the affinity is marginally increased with increasing van der Waals volume of the para-substituent:Log K(i)=-0.71sigma-(0.32)(0.	1-phenethylamine	60-83	monoamine oxidase B	Bos taurus	97-102
12371853-9	2002	At the same time, the parent 3-phenyl analogue is a pure substrate for the flavin-dependent mitochondrial monoamine oxidase B from bovine liver.	4,6-dinitro-o-cresol	75-81	monoamine oxidase B	Bos taurus	106-125
11049757-10	2000	Recombinant human liver MAO B and bovine liver MAO B are shown to be acetylated at the seryl residues at their respective amino termini.	seryl	87-92	monoamine oxidase B	Bos taurus	47-52
11049757-11	2000	The benzylamine oxidase activity of recombinant MAO B ranges from 3.0 to 3.4 U/mg and steady-state kinetic parameters for this enzyme preparation compare well with those published for the bovine liver enzyme: k(cat) = 600 min(-1), K(m)(benzylamine) = 0.50 mM, and K(m)(O(2)) = 0.33 mM.	benzylamine	4-15	monoamine oxidase B	Bos taurus	48-53
10445051-0	1999	Thiazole derivatives as inhibitors of purified bovine liver mitochondrial monoamine oxidase-B: structure-activity relationships and theoretical study.	Thiazoles	0-8	monoamine oxidase B	Bos taurus	74-93
10445051-1	1999	Structure-activity relationships were performed on a new series of thiazole derivatives which selectively inactivate monoamine oxidase-B (MAO-B), purified from mitochondrial beef liver.	Thiazoles	67-75	monoamine oxidase B	Bos taurus	117-136
10445051-1	1999	Structure-activity relationships were performed on a new series of thiazole derivatives which selectively inactivate monoamine oxidase-B (MAO-B), purified from mitochondrial beef liver.	Thiazoles	67-75	monoamine oxidase B	Bos taurus	138-143
10445051-3	1999	The mechanism of MAO-B inhibition is discussed in terms of the Ionization Potential of the amine nitrogen atom and the conformational flexibility of the inhibitors.	Amines	91-96	monoamine oxidase B	Bos taurus	17-22
10445051-3	1999	The mechanism of MAO-B inhibition is discussed in terms of the Ionization Potential of the amine nitrogen atom and the conformational flexibility of the inhibitors.	Nitrogen	97-105	monoamine oxidase B	Bos taurus	17-22
8954151-1	1996	The quaternary structure and subunit composition of bovine liver monoamine oxidase B (MAO B) was investigated using size-exclusion chromatography, sucrose gradient centrifugation and electron microscopy.	Sucrose	147-154	monoamine oxidase B	Bos taurus	65-84
8954151-1	1996	The quaternary structure and subunit composition of bovine liver monoamine oxidase B (MAO B) was investigated using size-exclusion chromatography, sucrose gradient centrifugation and electron microscopy.	Sucrose	147-154	monoamine oxidase B	Bos taurus	86-91
8954151-8	1996	Similarly, sucrose density gradient centrifugation of purified MAO B exhibited a direct correlation between enzyme activity and molecular mass of the MAO complexes.	Sucrose	11-18	monoamine oxidase B	Bos taurus	63-68
8954151-9	1996	MAO B activity was found to be widely distributed throughout the sucrose gradient and the highest enzyme activity was contained in the high-density sucrose layers.	Sucrose	65-72	monoamine oxidase B	Bos taurus	0-5
8954151-9	1996	MAO B activity was found to be widely distributed throughout the sucrose gradient and the highest enzyme activity was contained in the high-density sucrose layers.	Sucrose	148-155	monoamine oxidase B	Bos taurus	0-5
8954151-11	1996	Transmission electron microscopy of purified MAO B was performed using protein prepared by octyl glucoside extraction.	octyl-beta-D-glucoside	91-106	monoamine oxidase B	Bos taurus	45-50
8960870-4	1996	The monoamine oxidase (MAO) inhibitors pargyline (non-selective) and deprenyl (MAO-B-selective) have micromolar affinity for the I1-sites and much lower affinity for the I2-sites.	Selegiline	69-77	monoamine oxidase B	Bos taurus	79-84