1G4V
 
 | | ASPARTATE AMINOTRANSFERASE ACTIVE SITE MUTANT N194A/Y225F | | Descriptor: | ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Mizuguchi, H, Hayashi, H, Okada, K, Miyahara, I, Hirotsu, K, Kagamiyama, H. | | Deposit date: | 2000-10-28 | | Release date: | 2000-11-22 | | Last modified: | 2021-10-27 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase.
Biochemistry, 40, 2001
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1G7W
 | | ASPARTATE AMINOTRANSFERASE ACTIVE SITE MUTANT N194A/R386L | | Descriptor: | ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Mizuguchi, H, Hayashi, H, Okada, K, Miyahara, I, Hirotsu, K, Kagamiyama, H. | | Deposit date: | 2000-11-15 | | Release date: | 2000-11-29 | | Last modified: | 2021-10-27 | | Method: | X-RAY DIFFRACTION (2.2 Å) | | Cite: | Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase.
Biochemistry, 40, 2001
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1GCK
 | | THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1 COMPLEXED WITH ASPARTATE | | Descriptor: | ASPARTATE AMINOTRANSFERASE, ASPARTIC ACID, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Ura, H, Nakai, T, Hirotsu, K, Kuramitsu, S. | | Deposit date: | 2000-08-04 | | Release date: | 2001-11-14 | | Last modified: | 2023-12-27 | | Method: | X-RAY DIFFRACTION (2.5 Å) | | Cite: | Substrate recognition mechanism of thermophilic dual-substrate enzyme.
J.Biochem., 130, 2001
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1GDE
 | | CRYSTAL STRUCTURE OF PYROCOCCUS PROTEIN A-1 E-FORM | | Descriptor: | ASPARTATE AMINOTRANSFERASE, GLUTAMIC ACID, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Ura, H, Harata, K, Matsui, I, Kuramitsu, S. | | Deposit date: | 2000-09-23 | | Release date: | 2001-09-23 | | Last modified: | 2023-12-27 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | Temperature dependence of the enzyme-substrate recognition mechanism.
J.Biochem., 129, 2001
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1GEX
 | | CRYSTAL STRUCTURE OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH HISTIDINOL-PHOSPHATE | | Descriptor: | HISTIDINOL-PHOSPHATE AMINOTRANSFERASE, PHOSPHORIC ACID MONO-[2-AMINO-3-(3H-IMIDAZOL-4-YL)-PROPYL]ESTER, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Haruyama, K, Nakai, T, Miyahara, I, Hirotsu, K, Mizuguchi, H, Hayashi, H, Kagamiyama, H. | | Deposit date: | 2000-11-30 | | Release date: | 2001-04-18 | | Last modified: | 2023-12-27 | | Method: | X-RAY DIFFRACTION (2.2 Å) | | Cite: | Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme.
Biochemistry, 40, 2001
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1H1C
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1IAY
 | | CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH COFACTOR PLP AND INHIBITOR AVG | | Descriptor: | 1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE 2, 2-AMINO-4-(2-AMINO-ETHOXY)-BUTYRIC ACID, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Huai, Q, Xia, Y, Chen, Y, Callahan, B, Li, N, Ke, H. | | Deposit date: | 2001-03-24 | | Release date: | 2001-04-04 | | Last modified: | 2011-07-13 | | Method: | X-RAY DIFFRACTION (2.7 Å) | | Cite: | Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms
J.Biol.Chem., 276, 2001
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1J32
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1IX6
 | | Aspartate Aminotransferase Active Site Mutant V39F | | Descriptor: | Aspartate Aminotransferase, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Hayashi, H, Mizuguchi, H, Miyahara, I, Nakajima, Y, Hirotsu, K, Kagamiyama, H. | | Deposit date: | 2002-06-14 | | Release date: | 2002-07-03 | | Last modified: | 2023-12-27 | | Method: | X-RAY DIFFRACTION (2.2 Å) | | Cite: | Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis
J.BIOL.CHEM., 278, 2003
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1IVR
 | | STRUCTURE OF ASPARTATE AMINOTRANSFERASE | | Descriptor: | ASPARTATE AMINOTRANSFERASE, N-PYRIDOXYL-2,3-DIHYDROXYASPARTIC ACID-5-MONOPHOSPHATE | | Authors: | Graf Von Stosch, A. | | Deposit date: | 1996-10-11 | | Release date: | 1997-07-23 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (2.4 Å) | | Cite: | Aspartate aminotransferase complexed with erythro-beta-hydroxyaspartate: crystallographic and spectroscopic identification of the carbinolamine intermediate.
Biochemistry, 35, 1996
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1IAX
 | | CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH PLP | | Descriptor: | 1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE 2, PYRIDOXAL-5'-PHOSPHATE, SULFATE ION | | Authors: | Huai, Q, Xia, Y, Chen, Y, Callahan, B, Li, N, Ke, H. | | Deposit date: | 2001-03-24 | | Release date: | 2001-04-04 | | Last modified: | 2011-07-13 | | Method: | X-RAY DIFFRACTION (2.8 Å) | | Cite: | Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms
J.Biol.Chem., 276, 2001
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1IJI
 | | Crystal Structure of L-Histidinol Phosphate Aminotransferase with PLP | | Descriptor: | Histidinol Phosphate Aminotransferase, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Sivaraman, J, Li, Y, Larocque, R, Schrag, J.D, Cygler, M, Matte, A. | | Deposit date: | 2001-04-26 | | Release date: | 2001-08-29 | | Last modified: | 2017-10-04 | | Method: | X-RAY DIFFRACTION (2.2 Å) | | Cite: | Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate.
J.Mol.Biol., 311, 2001
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1LKC
 | | Crystal Structure of L-Threonine-O-3-Phosphate Decarboxylase from Salmonella enterica | | Descriptor: | 1,2-ETHANEDIOL, L-threonine-O-3-phosphate decarboxylase, PHOSPHATE ION, ... | | Authors: | Cheong, C.G, Bauer, C.B, Brushaber, K.R, Escalante-Semerena, J.C, Rayment, I. | | Deposit date: | 2002-04-24 | | Release date: | 2002-05-01 | | Last modified: | 2011-11-16 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica.
Biochemistry, 41, 2002
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1LC7
 | | Crystal Structure of L-Threonine-O-3-phosphate Decarboxylase from S. enterica complexed with a substrate | | Descriptor: | L-Threonine-O-3-Phosphate Decarboxylase, PHOSPHATE ION, PHOSPHOTHREONINE | | Authors: | Cheong, C.-G, Escalante-Semerena, J, Rayment, I. | | Deposit date: | 2002-04-05 | | Release date: | 2002-06-28 | | Last modified: | 2023-08-16 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: the apo, substrate, and product-aldimine complexes.
Biochemistry, 41, 2002
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1LC5
 | | Crystal Structure of L-Threonine-O-3-phosphate Decarboxylase from S. enterica in its apo state | | Descriptor: | L-Threonine-O-3-Phosphate Decarboxylase, PHOSPHATE ION | | Authors: | Cheong, C.-G, Escalante-Semerena, J, Rayment, I. | | Deposit date: | 2002-04-05 | | Release date: | 2002-06-28 | | Last modified: | 2023-08-16 | | Method: | X-RAY DIFFRACTION (1.46 Å) | | Cite: | Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: the apo, substrate, and product-aldimine complexes.
Biochemistry, 41, 2002
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1LC8
 | | Crystal Structure of L-Threonine-O-3-phosphate Decarboxylase from S. enterica complexed with its reaction intermediate | | Descriptor: | L-Threonine-O-3-Phosphate Decarboxylase, {3-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-2-METHYL-PROPYL}-PHOSPHONIC ACID | | Authors: | Cheong, C.-G, Escalante-Semerena, J, Rayment, I. | | Deposit date: | 2002-04-05 | | Release date: | 2002-06-28 | | Last modified: | 2023-08-16 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: the apo, substrate, and product-aldimine complexes.
Biochemistry, 41, 2002
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1IX8
 | | Aspartate Aminotransferase Active Site Mutant V39F/N194A | | Descriptor: | Aspartate Aminotransferase, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Hayashi, H, Mizuguchi, H, Miyahara, I, Nakajima, Y, Hirotsu, K, Kagamiyama, H. | | Deposit date: | 2002-06-14 | | Release date: | 2002-07-03 | | Last modified: | 2023-12-27 | | Method: | X-RAY DIFFRACTION (2.2 Å) | | Cite: | Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis
J.BIOL.CHEM., 278, 2003
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1IX7
 | | Aspartate Aminotransferase Active Site Mutant V39F maleate complex | | Descriptor: | Aspartate Aminotransferase, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Hayashi, H, Mizuguchi, H, Miyahara, I, Nakajima, Y, Hirotsu, K, Kagamiyama, H. | | Deposit date: | 2002-06-14 | | Release date: | 2002-07-03 | | Last modified: | 2023-12-27 | | Method: | X-RAY DIFFRACTION (2.2 Å) | | Cite: | Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis
J.BIOL.CHEM., 278, 2003
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1MAP
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1MAQ
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1M4N
 | | CRYSTAL STRUCTURE OF APPLE ACC SYNTHASE IN COMPLEX WITH [2-(AMINO-OXY)ETHYL](5'-DEOXYADENOSIN-5'-YL)(METHYL)SULFONIUM | | Descriptor: | (2-AMINOOXY-ETHYL)-[5-(6-AMINO-PURIN-9-YL)-3,4-DIHYDROXY-TETRAHYDRO-FURAN-2-YLMETHYL]-METHYL-SULFONIUM, 1-aminocyclopropane-1-carboxylate synthase, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... | | Authors: | Capitani, G, Eliot, A.C, Gut, H, Khomutov, R.M, Kirsch, J.F, Grutter, M.G. | | Deposit date: | 2002-07-03 | | Release date: | 2003-04-22 | | Last modified: | 2023-10-25 | | Method: | X-RAY DIFFRACTION (2.01 Å) | | Cite: | Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding.
BIOCHEM.BIOPHYS.ACTA PROTEINS & PROTEOMICS, 1647, 2003
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1M7Y
 | | Crystal structure of apple ACC synthase in complex with L-aminoethoxyvinylglycine | | Descriptor: | (2E,3E)-4-(2-aminoethoxy)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid, (4R)-2-METHYLPENTANE-2,4-DIOL, 1-aminocyclopropane-1-carboxylate synthase | | Authors: | Capitani, G, McCarthy, D, Gut, H, Gruetter, M.G, Kirsch, J.F. | | Deposit date: | 2002-07-23 | | Release date: | 2002-12-23 | | Last modified: | 2023-10-25 | | Method: | X-RAY DIFFRACTION (1.6 Å) | | Cite: | Apple 1-Aminocyclopropane-1-carboxylate Synthase in Complex with the Inhibitor
L-Aminoethoxyvinylglycine
J.Biol.Chem., 277, 2002
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8E9M
 | | Crystal structure of E. coli aspartate aminotransferase mutant VFIT bound to maleic acid at 278 K | | Descriptor: | Aspartate aminotransferase, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Chica, R.A, St-Jacques, A.D, Rodriguez, J.M, Thompson, M.C. | | Deposit date: | 2022-08-26 | | Release date: | 2022-10-05 | | Last modified: | 2023-10-18 | | Method: | X-RAY DIFFRACTION (1.76 Å) | | Cite: | Computational remodeling of an enzyme conformational landscape for altered substrate selectivity.
Nat Commun, 14, 2023
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8E9K
 | | Crystal structure of wild-type E. coli aspartate aminotransferase bound to maleate at 278 K | | Descriptor: | Aspartate aminotransferase, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Chica, R.A, St-Jacques, A.D, Rodriguez, J.M, Thompson, M.C. | | Deposit date: | 2022-08-26 | | Release date: | 2022-10-05 | | Last modified: | 2023-10-18 | | Method: | X-RAY DIFFRACTION (1.83 Å) | | Cite: | Computational remodeling of an enzyme conformational landscape for altered substrate selectivity.
Nat Commun, 14, 2023
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8E9S
 | | Crystal structure of E. coli aspartate aminotransferase mutant VFCS bound to maleic acid at 278 K | | Descriptor: | Aspartate aminotransferase, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Chica, R.A, St-Jacques, A.D, Rodriguez, J.M, Thompson, M.C. | | Deposit date: | 2022-08-26 | | Release date: | 2022-10-05 | | Last modified: | 2023-10-18 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | Computational remodeling of an enzyme conformational landscape for altered substrate selectivity.
Nat Commun, 14, 2023
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