Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase - Test2 - elhamkhani - TriplyDB

Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase

Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase

http://www.wikidata.org/entity/Q27765259

about

The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step The structure ofPseudomonasP51 Cl-muconate lactonizing enzyme: Co-evolution of structure and dynamics with the dehalogenation function The structural determination of phosphosulfolactate synthase from Methanococcus jannaschii at 1.7-A resolution: an enolase that is not an enolase Evolution of Enzymatic Activities in the Enolase Superfamily: Stereochemically Distinct Mechanisms in Two Families of cis , cis -Muconate Lactonizing Enzymes † ‡The TIM-barrel fold: a versatile framework for efficient enzymes Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis. Mutational and structural characterization of the active site and the fold Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold.FAST-NMR: functional annotation screening technology using NMR spectroscopy Gene cluster of Arthrobacter ilicis Ru61a involved in the degradation of quinaldine to anthranilate: characterization and functional expression of the quinaldine 4-oxidase qoxLMS genes.Mutations in catB, the gene encoding muconate cycloisomerase, activate transcription of the distal ben genes and contribute to a complex regulatory circuit in Acinetobacter sp. strain ADP1.Functional evolution of PLP-dependent enzymes based on active-site structural similarities Expanding protein universe and its origin from the biological Big Bang.Evolutionary migration of a post-translationally modified active-site residue in the proton-pumping heme-copper oxygen reductases.Using catalytic atom maps to predict the catalytic functions present in enzyme active sites.FINDSITE: a combined evolution/structure-based approach to protein function prediction Directed evolution of a (beta alpha)8-barrel enzyme to catalyze related reactions in two different metabolic pathways.A domain for editing by an archaebacterial tRNA synthetase Sequence-Based Screening for Rare Enzymes: New Insights into the World of AMDases Reveal a Conserved Motif and 58 Novel Enzymes Clustering in Eight Distinct Families.Modeling regionalized volumetric differences in protein-ligand binding cavities.Finding evolutionary relations beyond superfamilies: fold-based superfamilies Characterization of a novel Agrobacterium tumefaciens galactarolactone cycloisomerase enzyme for direct conversion of D-galactarolactone to 3-deoxy-2-keto-L-threo-hexarate.The novel catabolic pathway of 3,6-anhydro-L-galactose, the main component of red macroalgae, in a marine bacterium.Automated selection of positions determining functional specificity of proteins by comparative analysis of orthologous groups in protein families.

P2860

Q27636942-055E866E-F6E1-449C-8A13-8FCC6766C651 Q27641881-D5C1283A-D53D-41A4-8843-FE87B2E7A5B0 Q27641945-8DEC1EA2-03C0-466B-B063-FDAC7D7E8DBB Q27653827-397C5AAB-34CD-45C8-811D-CDFADC8122EA Q28205462-C4E7415C-4858-4863-8370-83B104A11C04 Q28486954-FA0B07FC-B02E-4DAE-A355-D9E90A85C6DB Q30175241-DD02EC39-4EFB-43AE-9A63-43BD12768B90 Q30358176-9F854D9F-9BDF-4DBA-85DE-325FB0FF80B4 Q31141244-14CC2484-1F4C-4B41-B990-5CBE7A41B384 Q33995088-5E37C39E-ABFF-4442-B307-A004D30ADAAD Q34254917-9CA3C136-08A8-4D37-9437-2B7057E00DB4 Q34392268-17D189CF-C95D-4804-B94A-B5FE1224F58E Q34592277-6E3B0FF2-F859-46F2-98A4-EAE0ED77B166 Q36266742-26EDC96D-FFD9-4124-9BAF-4E4FF6D30E98 Q37215648-F25D3E07-9B5E-4BEC-A589-125B77EF702B Q37389262-93E7B64A-439B-4500-86C6-ADA439F8B9DD Q37646125-99606C17-57DA-4F86-BD5D-E62B89E69AD2 Q39408197-15F3AD3C-4233-40C8-9E2C-EA421137133A Q41889970-9D64C4D6-A47A-4494-B5CB-070ABA42821A Q41984013-33F57FD1-10C5-4113-998E-3551C946310C Q42183574-C9740418-6D70-4406-A171-E6785856538F Q42704375-F4F09DF3-E738-4311-9D2B-2C813A54E6FC Q43105221-D53DDD80-0918-4EE6-A2B5-BE11FB5B60CE

P2860

Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase

http://www.wikidata.org/entity/Q27765259

description

1998 nî lūn-bûn

@nan

1998 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

1998年の論文

@ja

1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

name

Evolution of an enzyme active ...... mandelate racemase and enolase

@ast

Evolution of an enzyme active ...... mandelate racemase and enolase

@en

Evolution of an enzyme active ...... mandelate racemase and enolase

@nl

type

label

Evolution of an enzyme active ...... mandelate racemase and enolase

@ast

Evolution of an enzyme active ...... mandelate racemase and enolase

@en

Evolution of an enzyme active ...... mandelate racemase and enolase

@nl

prefLabel

Evolution of an enzyme active ...... mandelate racemase and enolase

@ast

Evolution of an enzyme active ...... mandelate racemase and enolase

@en

Evolution of an enzyme active ...... mandelate racemase and enolase

@nl

P1433

Q27765259-0BC7E4EB-8E7F-47AC-8A5D-15C415EF7BA5

P1476

Q27765259-E0F8BB7E-CE02-4859-865E-5715340FA0A3

P2093

Q27765259-30C58947-5DAD-478D-B0FF-03CC355186EA

Q27765259-315C81B2-9533-4855-A24C-EE72C7C6E287

Q27765259-3EB76FAD-7B57-4893-80F1-4F3FEAB260A0

Q27765259-81CAD41E-B4B5-4450-A987-630A7D85557B

Q27765259-D9897F63-034C-4EEA-BF0E-03FCE87AC49A

Q27765259-DC3192D0-A067-4393-924F-5847393867B8

Q27765259-E6354A34-F479-4C8B-850C-D2753ED77263

Q27765259-F3396925-4F94-4A27-81A6-BD09FB9720BC

P2860

Q27765259-04C81ADF-DC92-48B4-9FCD-8F2548597654

Q27765259-07462111-C01B-49E7-84D7-6B74D45664A3

Q27765259-1606B889-67AD-4333-A963-0591653CE7D0

Q27765259-1717D500-7D42-4C86-8574-284D97CE8510

Q27765259-176CF925-3990-435D-9B1A-C09F18AEA795

Q27765259-3CCE3CFF-E4C4-4831-8178-4D2EC215798F

Q27765259-422CDBB5-C30A-4C2E-AD5A-4E1936BCF164

Q27765259-47401940-7442-4B47-8408-1265DEBCD79D

Q27765259-4BC1D74A-89D6-4FA7-A18F-91EA17058EF1

Q27765259-4C96892C-BE76-4383-936F-FA8E9FA434E7

P304

Q27765259-CF49439B-8A08-4D95-A21F-85166C295E68

P31

Q27765259-B8807E80-FD2F-4F45-AB24-0AB066276363

P3181

Q27765259-94F40546-26C8-45C6-AAC5-28C1979563A3

P356

Q27765259-5A888101-C20D-4DBE-93E8-6F677DF6F582

P407

Q27765259-FBDCE2AC-DDDC-4285-A3B1-642CBDBA3837

P433

Q27765259-8E937069-7579-42CF-8529-8DA5CE8CD1F9

P478

Q27765259-CC5AA8C6-7235-4EA8-9048-4772198E9D69

P50

Q27765259-A8A60772-F298-4BCD-8688-A6149F0DC6C8

Q27765259-F920707F-4231-4EE9-A704-8EEEA2D62227

P577

Q27765259-31DB70AD-0AFD-4735-ADCB-38D5D79ED7AB

P5875

Q27765259-98BB848B-65AB-4FEC-B05F-A81288043225

P698

Q27765259-72383961-2E3C-426B-A4C7-BB8E58932715

P932

Q27765259-D589C3FB-E7F5-4AA9-8795-F9B53E9F7A1A

P3181

P356

PNAS.95.18.10396

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Evolution of an enzyme active ...... mandelate racemase and enolase

@en

P2093

G L Kenyon

http://www.w3.org/2001/XMLSchema#string

I Schlichting

http://www.w3.org/2001/XMLSchema#string

J A Gerlt

http://www.w3.org/2001/XMLSchema#string

J Moulai

http://www.w3.org/2001/XMLSchema#string

K Taylor

http://www.w3.org/2001/XMLSchema#string

M S Hasson

http://www.w3.org/2001/XMLSchema#string

P C Babbitt

http://www.w3.org/2001/XMLSchema#string

W Barrett

http://www.w3.org/2001/XMLSchema#string

P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

A comprehensive set of sequence analysis programs for the VAX

Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-A resolution: identification of the active site and possible catalytic residues

The refined X-ray structure of muconate lactonizing enzyme from Pseudomonas putida PRS2000 at 1.85 A resolution

Octahedral coordination at the high-affinity metal site in enolase: crystallographic analysis of the MgII--enzyme complex from yeast at 1.9 A resolution

Chelation of serine 39 to Mg2+ latches a gate at the active site of enolase: structure of the bis(Mg2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-A resolution

A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution

The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes

Solvent content of protein crystals

P304

10396-401

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

3883606

http://www.w3.org/2001/XMLSchema#string

P356

10.1073/PNAS.95.18.10396

http://www.w3.org/2001/XMLSchema#string

P407

P433

18

http://www.w3.org/2001/XMLSchema#string

P478

95

http://www.w3.org/2001/XMLSchema#string

P50

P577

1998-09-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

235609456

http://www.w3.org/2001/XMLSchema#string

P698

9724714

http://www.w3.org/2001/XMLSchema#string

P932

27905

http://www.w3.org/2001/XMLSchema#string