Conformation and reaction specificity in pyridoxal phosphate enzymes.
about
Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effectsStructural study reveals that Ser-354 determines substrate specificity on human histidine decarboxylaseAldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolaseCrystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnusX-ray structure determination of Trypanosoma brucei ornithine decarboxylase bound to D-ornithine and to G418: insights into substrate binding and ODC conformational flexibilityRapid Synthesis of Auxin via a New Tryptophan-Dependent Pathway Is Required for Shade Avoidance in PlantsProbing the Active Center of Benzaldehyde Lyase with Substitutions and the Pseudosubstrate Analogue Benzoylphosphonic Acid Methyl Ester †The External Aldimine Form of Serine Palmitoyltransferase: STRUCTURAL, KINETIC, AND SPECTROSCOPIC ANALYSIS OF THE WILD-TYPE ENZYME AND HSAN1 MUTANT MIMICSStructural insights into the enzymatic mechanism of serine palmitoyltransferase from Sphingobacterium multivorumDouble Duty for a Conserved Glutamate in Pyruvate Decarboxylase: Evidence of the Participation in Stereoelectronically Controlled Decarboxylation and in Protonation of the Nascent Carbanion/Enamine Intermediate,Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecyStructural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine -synthaseProduct-assisted Catalysis as the Basis of the Reaction Specificity of Threonine SynthaseLinkage between the bacterial acid stress and stringent responses: the structure of the inducible lysine decarboxylaseCrystal Structure of a Zinc-dependent D-Serine Dehydratase from Chicken KidneyCrystallographic Snapshots of Tyrosine Phenol-lyase Show That Substrate Strain Plays a Role in C–C Bond CleavageThe Last Piece in the Vitamin B1 Biosynthesis Puzzle: STRUCTURAL AND FUNCTIONAL INSIGHT INTO YEAST 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE PHOSPHATE (HMP-P) SYNTHASECrystal structures of the Chromobacterium violaceumω-transaminase reveal major structural rearrangements upon binding of coenzyme PLPStructural studies ofPseudomonasandChromobacteriumω-aminotransferases provide insights into their differing substrate specificityKinetic, Mutational, and Structural Analysis of Malonate Semialdehyde Decarboxylase from Coryneform Bacterium Strain FG41: Mechanistic Implications for the Decarboxylase and Hydratase ActivitiesGround-State Electronic Destabilization via Hyperconjugation in Aspartate AminotransferaseStructural insights into catalysis by βC-S lyase from Streptococcus anginosusStructure of the Homodimeric Glycine Decarboxylase P-protein from Synechocystis sp. PCC 6803 Suggests a Mechanism for Redox RegulationCrystal structure and substrate specificity of the thermophilic serine:pyruvate aminotransferase from Sulfolobus solfataricusThe substrate specificity, enantioselectivity and structure of the (R)-selective amine : pyruvate transaminase fromNectria haematococcaFrom cofactor to enzymes. The molecular evolution of pyridoxal-5'-phosphate-dependent enzymesNMR Crystallography of a Carbanionic Intermediate in Tryptophan Synthase: Chemical Structure, Tautomerization, and Reaction SpecificityMolecular evolution of B6 enzymes: binding of pyridoxal-5'-phosphate and Lys41Arg substitution turn ribonuclease A into a model B6 protoenzyme.NMR crystallography of enzyme active sites: probing chemically detailed, three-dimensional structure in tryptophan synthaseThe structure of Plasmodium falciparum serine hydroxymethyltransferase reveals a novel redox switch that regulates its activities.Defining critical residues for substrate binding to 1-deoxy-D-xylulose 5-phosphate synthase--active site substitutions stabilize the predecarboxylation intermediate C2α-lactylthiamin diphosphate.Control of lysine biosynthesis in Bacillus subtilis: inhibition of diaminopimelate decarboxylase by lysine5-aminolevulinate synthase: catalysis of the first step of heme biosynthesisUnstable reaction intermediates and hysteresis during the catalytic cycle of 5-aminolevulinate synthase: implications from using pseudo and alternate substrates and a promiscuous enzyme variant.Role of a conserved arginine residue during catalysis in serine palmitoyltransferase.Functional evolution of PLP-dependent enzymes based on active-site structural similaritiesMutational analysis of substrate interactions with the active site of dialkylglycine decarboxylaseLight-enhanced catalysis by pyridoxal phosphate-dependent aspartate aminotransferase.Structural biology of plant sulfur metabolism: from assimilation to biosynthesis.Mechanistic studies of 1-aminocyclopropane-1-carboxylate deaminase: characterization of an unusual pyridoxal 5'-phosphate-dependent reaction.
P2860
Q22254069-E28D3239-BFC5-439E-8122-FFD80DAEDEB0Q24339546-3DB34D67-07C2-4B55-8E4A-14A38F08E0B7Q24531292-ECADFD48-DF72-42B3-815D-EC5EF47C6774Q27626428-B9EE9A13-41FC-4F1B-95A3-E02E627E5592Q27640879-8416752C-A877-40A5-BC54-CA92FB1A8E10Q27650264-64F40656-F43B-4A19-8A67-EFBB546A2259Q27650916-CC1EABBE-461F-4E50-9066-60565E9907A2Q27654958-17F7F0BF-220C-4CEB-9ED5-BB9ED6A553AFQ27656285-C8F9CA16-7934-4D98-BC44-369B9AFD1584Q27664071-F1372463-035B-4EA7-9F02-FFD75073059FQ27665873-E01E5F42-7E9D-4D3C-B1A9-E44B5602E01AQ27665916-46A6C44D-6D43-4A53-A2F8-99839B919CE7Q27665954-508A904D-5FF7-46CC-9607-E21940925BD7Q27666777-3E50F70C-C7D1-4523-9CF7-DD180C28CBF2Q27670452-516AC31C-51EA-4A93-A167-68B9BE0E601DQ27673385-9A312275-89BA-4B2C-9EAE-4410685C0537Q27674366-6D6AB077-6B42-4D61-AF16-87DB3A4D796BQ27676850-D76EB8DE-2B5F-4E88-A943-9F5CCC399CCBQ27676955-D6296DC5-C9D0-467C-8AB0-EA984642B34BQ27678700-C5315F21-4F47-4C52-8D24-143575ECE823Q27678869-11A23145-EC3B-4092-A866-1ED5A0078079Q27679522-3B2CAB00-BD7B-4152-B3EE-2AD7C5C83CB7Q27680306-1B67E14B-2DB5-4890-B455-355BC0E8E9CCQ27681673-A6194A53-2BE4-44F7-B159-06E9BCE2032AQ27682128-2F6446B0-699F-4AED-B073-8E91DEA30536Q28212888-A400BAC7-8127-44D6-8983-AFA54C7AD155Q28818305-5EA49EEE-AE2E-41AD-9FF4-61966F7FDEBFQ33345009-0EB9B017-1562-45F7-8BA1-FD375D660B0DQ33355538-12532081-46B7-40EA-A2B2-94E1C08F4EE0Q33733595-426E0FBB-B758-47A6-957C-36987B124252Q33785548-A22086D3-A2A9-4E39-BDCA-E0F8A2EF4F96Q33795180-9EFD6A65-6F4D-4B15-8BE2-B33BD87DE05EQ33830495-D9D8995B-DEDE-4414-8FDB-9163DFF00B84Q34044659-AFAB27CC-A410-4271-9B91-2C7DB2FAB562Q34180063-89250501-8F60-4FD1-82DA-D703D0D69A30Q34254917-B817A578-D099-424A-B383-2655573A6AAAQ34366533-5CA72ECF-A149-4E8F-8C47-22AE484A8B06Q34496057-F4FF8C1F-40A4-403D-BA6B-6A16D352E735Q34638385-6F62A301-94B9-4EE5-A861-240B8AFEC35DQ34687196-94B7DB78-2B50-4FB4-B3E3-2C839A5C4852
P2860
Conformation and reaction specificity in pyridoxal phosphate enzymes.
description
1966 nî lūn-bûn
@nan
1966年の論文
@ja
1966年学术文章
@wuu
1966年学术文章
@zh-cn
1966年学术文章
@zh-hans
1966年学术文章
@zh-my
1966年学术文章
@zh-sg
1966年學術文章
@yue
1966年學術文章
@zh
1966年學術文章
@zh-hant
name
Conformation and reaction specificity in pyridoxal phosphate enzymes.
@ast
Conformation and reaction specificity in pyridoxal phosphate enzymes.
@en
type
label
Conformation and reaction specificity in pyridoxal phosphate enzymes.
@ast
Conformation and reaction specificity in pyridoxal phosphate enzymes.
@en
prefLabel
Conformation and reaction specificity in pyridoxal phosphate enzymes.
@ast
Conformation and reaction specificity in pyridoxal phosphate enzymes.
@en
P2860
P356
P1476
Conformation and reaction specificity in pyridoxal phosphate enzymes.
@en
P2093
Dunathan HC
P2860
P304
P356
10.1073/PNAS.55.4.712
P407
P577
1966-04-01T00:00:00Z