Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity
about
Characterization of the genes encoding D-amino acid transaminase and glutamate racemase, two D-glutamate biosynthetic enzymes of Bacillus sphaericus ATCC 10208Crystal Structure of an (R)-Selective ω-Transaminase from Aspergillus terreusCrystallographic characterization of the (R)-selective amine transaminase from Aspergillus fumigatusCrystal structures of two tropinone reductases: different reaction stereospecificities in the same protein foldTwo yeast homologs of ECA39, a target for c-Myc regulation, code for cytosolic and mitochondrial branched-chain amino acid aminotransferases.Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentinFrom cofactor to enzymes. The molecular evolution of pyridoxal-5'-phosphate-dependent enzymesOverexpression and characterization of the human mitochondrial and cytosolic branched-chain aminotransferasesLysine 2,3-aminomutase from Clostridium subterminale SB4: mass spectral characterization of cyanogen bromide-treated peptides and cloning, sequencing, and expression of the gene kamA in Escherichia coli.Functional evolution of PLP-dependent enzymes based on active-site structural similaritiesCrystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function.Stereospecificity for the hydrogen transfer of pyridoxal enzyme reactions.Release of enzyme strain during catalysis reduces the activation energy barrier.Substituent effects on electrophilic catalysis by the carbonyl group: anatomy of the rate acceleration for PLP-catalyzed deprotonation of glycine.Glutamate Racemase Mutants of Bacillus anthracis.Cloning, purification, and crystallization of Escherichia coli cystathionine beta-lyase.Cytoplasmic steps of peptidoglycan biosynthesis.Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme foldPyridoxal 5'-phosphate: electrophilic catalyst extraordinaire.The PLP cofactor: lessons from studies on model reactions.Cloning and expression of the mammalian cytosolic branched chain aminotransferase isoenzyme.Chemogenomics of pyridoxal 5'-phosphate dependent enzymes.Stereochemical constraint in the evolution of pyridoxal-5'-phosphate-dependent enzymes. A hypothesis.Catalytic ability and stability of two recombinant mutants of D-amino acid transaminase involved in coenzyme binding.The ubiquitous cofactor NADH protects against substrate-induced inhibition of a pyridoxal enzyme.Functional and structural characterization of thermostable D-amino acid aminotransferases from Geobacillus spp.Site-directed mutagenesis of the amino acid residues in beta-strand III [Val30-Val36] of D-amino acid aminotransferase of Bacillus sp. YM-1.Cloning and functional characterization of Arabidopsis thaliana D-amino acid aminotransferase--D-aspartate behavior during germination.Purification and cloning of the mitochondrial branched-chain amino acid aminotransferase from sheep placenta.Structure and function of the tryptophan synthase alpha(2)beta(2) complex. Roles of beta subunit histidine 86.Synthesis of Chiral Amines Using Transaminases
P2860
Q24521456-779A930F-17A2-4648-8D25-B2FDC216EF8EQ27681585-0F8FA61B-C00B-432D-A7F4-436BD8A943A9Q27689937-D60661F8-D20D-4605-A4D7-96C8198AF74EQ27749621-004D5174-BF92-42B8-93D6-AED4BC10DE42Q27934610-D3E72A75-A623-4362-AA5D-38F668D5D8BBQ28115621-325ABCEF-3025-4339-99BE-EBF1A474B070Q28212888-44B3F625-6D26-4181-B0C1-0AB137947055Q28262954-881301FF-E39A-4BCB-9265-B133930E6390Q30832029-F24446B1-C9CF-4AC3-9F53-D7BA03C7EC67Q34254917-F5AAAC41-BC28-4877-943E-277B7436B74AQ34336613-FE5D253E-C589-4C42-8669-F7FC0988FC79Q34587643-3DF868E2-B968-4825-B67A-6B63ADA62806Q34587651-9FD3D588-0445-42B9-8AF9-C69ECFF2F24EQ34698692-7AF31953-04BE-49AD-88B1-41200A897F36Q35572969-25731A97-0FE1-416C-A2EF-1FFD45235BCEQ36791465-1FCE5846-2F45-4845-A4F6-6DF74EFA0969Q37081699-4AFCBE0E-7890-4A2D-972B-49086B81C6BDQ37460042-E244C232-36D4-458D-9BFA-4021071E227BQ37565896-C728790F-BA8A-44FC-8D6D-3BC2987EBF5FQ37823717-9E03A76E-9137-479B-B943-B98AA3CCD373Q38287830-F8540973-5588-4356-BE3E-B79B82F607BCQ39674260-D40E40A3-3370-4C5C-A129-35519F49FFF4Q41017031-DBCBA7E0-0CE5-4064-A7F9-230010F0C397Q41895452-BF388102-E4DD-472E-A418-B9F795A6ABD7Q42116415-F8BE373F-4B0E-4FEE-82BA-AFA5E1E09C6AQ42122309-A4CE4502-43B6-4651-9448-1895BC19369AQ43024362-4FA10445-106A-4A8F-A2F2-8F96E1F152D2Q46719498-FDAE506D-6BF9-496D-9914-729173DA1D53Q47993225-BFD61888-4EC1-4350-9414-8BADE4CADAA3Q50123224-B7948FEF-EB45-43D8-B5D7-4D8B616FDCD2Q58048704-D9D3208D-6C34-4E75-8391-66A2C1C6E692
P2860
Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity
description
1995 nî lūn-bûn
@nan
1995 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Crystal structure of a D-amino ...... ein controls stereoselectivity
@ast
Crystal structure of a D-amino ...... ein controls stereoselectivity
@en
Crystal structure of a D-amino ...... ein controls stereoselectivity
@nl
type
label
Crystal structure of a D-amino ...... ein controls stereoselectivity
@ast
Crystal structure of a D-amino ...... ein controls stereoselectivity
@en
Crystal structure of a D-amino ...... ein controls stereoselectivity
@nl
prefLabel
Crystal structure of a D-amino ...... ein controls stereoselectivity
@ast
Crystal structure of a D-amino ...... ein controls stereoselectivity
@en
Crystal structure of a D-amino ...... ein controls stereoselectivity
@nl
P2093
P356
P1433
P1476
Crystal structure of a D-amino ...... ein controls stereoselectivity
@en
P2093
P304
P356
10.1021/BI00030A002
P407
P577
1995-08-01T00:00:00Z