An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily - Wikidata - awgldk - TriplyDB

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily

http://www.wikidata.org/entity/Q27659538

about

Structure of sulfamidase provides insight into the molecular pathology of mucopolysaccharidosis IIIA Computational protein engineering: bridging the gap between rational design and laboratory evolution.Structure of a lipid A phosphoethanolamine transferase suggests how conformational changes govern substrate binding The alkaline hydrolysis of sulfonate esters: challenges in interpreting experimental and theoretical data Divergence and convergence in enzyme evolution.A measure of the promiscuity of proteins and characteristics of residues in the vicinity of the catalytic site that regulate promiscuity.QM/MM analysis suggests that Alkaline Phosphatase (AP) and nucleotide pyrophosphatase/phosphodiesterase slightly tighten the transition state for phosphate diester hydrolysis relative to solution: implication for catalytic promiscuity in the AP supe Escherichia coli D-malate dehydrogenase, a generalist enzyme active in the leucine biosynthesis pathway Enzyme promiscuity: engine of evolutionary innovation.A measure of the broad substrate specificity of enzymes based on 'duplicate' catalytic residues A computational module assembled from different protease family motifs identifies PI PLC from Bacillus cereus as a putative prolyl peptidase with a serine protease scaffold Model-driven discovery of underground metabolic functions in Escherichia coli Site-directed mutagenesis maps interactions that enhance cognate and limit promiscuous catalysis by an alkaline phosphatase superfamily phosphodiesterase.Cooperative Electrostatic Interactions Drive Functional Evolution in the Alkaline Phosphatase Superfamily.Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.The Competing Mechanisms of Phosphate Monoester Dianion Hydrolysis Specificity Effects of Amino Acid Substitutions in Promiscuous Hydrolases: Context-Dependence of Catalytic Residue Contributions to Local Fitness Landscapes in Nearby Sequence Space.Enzyme sub-functionalization driven by regulation.Stabilization of different types of transition states in a single enzyme active site: QM/MM analysis of enzymes in the alkaline phosphatase superfamily.Facilitating the Evolution of Esterase Activity from a Promiscuous Enzyme (Mhg) with Catalytic Functions of Amide Hydrolysis and Carboxylic Acid Perhydrolysis by Engineering the Substrate Entrance Tunnel.High resolution crystal structure of the catalytic domain of MCR-1.Active Site Hydrophobicity and the Convergent Evolution of Paraoxonase Activity in Structurally Divergent Enzymes: The Case of Serum Paraoxonase 1.Why nature really chose phosphate.Flexibility and reactivity in promiscuous enzymes.Dynamics and constraints of enzyme evolution.Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications.The Streptomyces-produced antibiotic fosfomycin is a promiscuous substrate for archaeal isopentenyl phosphate kinase.Perspectives for biocatalytic lignin utilization: cleaving 4-O-5 and Cα-Cβ bonds in dimeric lignin model compounds catalyzed by a promiscuous activity of tyrosinase Mechanistic and Evolutionary Insights from Comparative Enzymology of Phosphomonoesterases and Phosphodiesterases across the Alkaline Phosphatase Superfamily Modeling catalytic promiscuity in the alkaline phosphatase superfamily.Catalytic zinc complexes for phosphate diester hydrolysis.Probing the origins of catalytic discrimination between phosphate and sulfate monoester hydrolysis: comparative analysis of alkaline phosphatase and protein tyrosine phosphatases.A 1-year study of the activities of seven hydrolases in a communal wastewater treatment plant: trends and correlations.Kinetic and computational evidence for an intermediate in the hydrolysis of sulfonate esters.Differential catalytic promiscuity of the alkaline phosphatase superfamily bimetallo core reveals mechanistic features underlying enzyme evolution.Structural and Mechanistic Analysis of the Choline Sulfatase from Sinorhizobium melliloti: A Class I Sulfatase Specific for an Alkyl Sulfate Ester.In Vitro Reconstitution of Formylglycine-Generating Enzymes Requires Copper(I).Inhibition of a cold-active alkaline phosphatase by imipenem revealed by in silico modeling of metallo-β-lactamase active sites.

P2860

Q27683714-145D4E91-D1E1-4A4D-9B2B-76643E49830C Q30394571-FC8805C9-B78D-4A66-8111-033B08169255 Q30398553-B5D1684D-D554-41F9-9000-39C2DB7C84F0 Q30702060-0149D6FE-8469-4DDF-ABAE-A46BD907FAA9 Q34070421-43C4B908-75A4-4869-850D-CC781D9D6C72 Q34168526-9F8C1A00-E145-4B80-BB85-2B5B73A419A4 Q34234062-13BA1D24-436D-4488-B193-0F5AFB302983 Q34355701-9DB8FE59-A7F1-42F0-9B89-403BC668A216 Q34430867-2711A055-781D-41D9-8906-723BB5A93800 Q34482204-4DA806D0-FD43-488A-BD97-5EA349238711 Q34936357-6156A65D-1607-437D-B9B4-3B01FAC8F71C Q35031478-A7105E83-6267-4586-910C-5B96059752CC Q35558012-ED946BF2-64E8-49B9-80FB-03DE0FCD03E5 Q35669041-EFE3A5D7-95AA-422B-9CD4-20F4362C1CE8 Q36019839-364409F8-BD88-4689-B039-236D4794D5D7 Q36089437-F80CC592-ADEB-479E-8373-86BB162F4F70 Q36360999-EF4208BE-0B6F-47C9-90BC-A878FB985787 Q36405739-9610B341-FB7E-4F98-A621-12C4011F1028 Q37137337-3209F2DB-F09F-474C-8FBC-FE50B534ADF6 Q37378711-6F8C4DA5-7EB8-4D18-A00C-13E0ABADC7D6 Q37522439-31E91A43-122A-462C-997B-E0F9AC662D62 Q37609374-651601AA-4C45-43DF-B2A2-D44A5769C0B5 Q38073986-2D2F6DFA-95BB-41DA-B756-163E316F488F Q38077741-4B9B7955-AA83-410D-BDC1-1420E23B4029 Q38187602-D5967295-1813-4696-BDE3-F2A8210203DD Q38287400-36794E91-1896-4428-B066-1ADF0650CE15 Q38290367-1412DABA-D22B-477B-9B7D-C94DBAFDEFC4 Q40892454-6D2057DE-2FB8-4558-B176-652F77AFC7C5 Q41283098-D063E3F2-059F-48B2-960D-13A756BA2B73 Q41676786-7F21AA53-4AAA-4B13-91C9-6979535290F8 Q42024162-6F437C62-5D1F-4F59-9630-3EF48AF6D917 Q42152654-BC79B187-94E1-4516-A364-1FAEB64725D4 Q42549522-C4A01CF3-FDF2-4CC9-8CF0-DB90683EE62F Q43348091-E34349B3-A85A-4152-9FEF-D6FAD82564E4 Q45858883-752EC162-0105-440C-863E-4DE0E9E71C8F Q47410126-250CB1C0-1EB7-4381-BA31-E43333543946 Q49847175-2233D7F0-4544-495E-AA53-806988931730 Q51708942-561C2AA5-763E-4424-9914-6C0654B4552A Q54327863-2DE4062F-C658-4170-B140-0A87AE9886BD

P2860

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily

http://www.wikidata.org/entity/Q27659538

description

2010 nî lūn-bûn

@nan

2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily

@ast

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily

@en

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily

@nl

type

label

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily

@ast

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily

@en

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily

@nl

prefLabel

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily

@ast

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily

@en

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily

@nl

P1433

Q27659538-83B3A57F-8A6C-4536-AF53-00679F564E2D

P1476

Q27659538-67BDDFDB-2363-4A65-A936-50863B8F4358

P2093

Q27659538-038EA642-AED0-4372-A1E2-AD6C908195B0

Q27659538-0E568813-241F-4EBD-A2F1-37A8FFEC8763

Q27659538-C965A135-905F-4E8E-A5FC-1B3157E4587D

P2860

Q27659538-335020F4-E345-4C33-B130-B9C13E16C934

Q27659538-3392609F-FC18-474A-800D-B82E66C0731D

Q27659538-34E6D42E-798C-4D9C-84F2-892AB9BF2232

Q27659538-34F5A194-F67E-41C0-AF3F-184141D54A95

Q27659538-40DD99C5-1791-442B-9016-79743078B0FF

Q27659538-42856A7F-0EED-484D-BC60-807C03E74D78

Q27659538-44B1B31C-D1B7-449B-B825-527E64BB7EB5

Q27659538-4A96C19C-3A6C-44E4-8153-519FE286B2EC

Q27659538-4FD77ADE-DAD1-40FF-AF87-0B6B0368EC38

Q27659538-5229024C-CEB1-4097-910C-D21225D56971

P304

Q27659538-EB6E2D41-6E1C-4993-AE12-85F8E5A5874C

P31

Q27659538-0E79A651-1F90-4BA6-BD81-AA81F20A0096

P3181

Q27659538-DFDB2170-4149-4D09-ACE7-B6BC631238F0

P356

Q27659538-12C9E983-A2FD-48A4-8991-0EB6304BFD4A

P407

Q27659538-4CA55D6B-2110-4CFD-9BA1-B02E86AA3C51

P433

Q27659538-2D493CF5-FB13-40C3-9AC9-F67D577D88C9

P478

Q27659538-200EEA23-8D92-45F3-8C95-180FE76795FE

P50

Q27659538-2624ADC9-5D6C-4E41-9704-12C365017777

Q27659538-39CC0B30-C61F-4A73-B86F-7861B2A23291

Q27659538-985B403D-B470-4347-8070-F192983084EA

Q27659538-E24758D4-874C-45F9-B558-C17AF0BE31D5

P577

Q27659538-833BC072-4D17-4976-8EB8-0B65B59C6FF5

P5875

Q27659538-141E6169-36CF-4C4E-BAB1-E5EB51D37F36

P698

Q27659538-3D20E6A3-0CBB-4914-B3E0-688DC8CD3B7C

P932

Q27659538-7E7A2143-2B43-4176-AB13-BAB35C2C6CE6

P3181

P356

PNAS.0903951107

P1433

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

P1476

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily

@en

P2093

Alhosna Benjdia

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

Ann C Babtie

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

Marko Hyvönen

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

P2860

Alkaline phosphatase mono- and diesterase reactions: comparative transition state analysis

A new member of the alkaline phosphatase superfamily with a formylglycine nucleophile: structural and kinetic characterisation of a phosphonate monoester hydrolase/phosphodiesterase from Rhizobium leguminosarum

The interpretation of protein structures: estimation of static accessibility

A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases

Catalytic promiscuity and the evolution of new enzymatic activities

A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency

The 'evolvability' of promiscuous protein functions

Introducing genetically encoded aldehydes into proteins

Minimalist active-site redesign: teaching old enzymes new tricks

The Rv0805 gene from Mycobacterium tuberculosis encodes a 3',5'-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis

P304

2740-5

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

P31

scholarly article

P3181

1595375

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

P356

10.1073/PNAS.0903951107

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

P407

P433

7

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

P478

107

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

P50

Florian Hollfelder

Olivier Berteau

P577

2010-02-16T00:00:00Z

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

P5875

41408465

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

P698

20133613

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

P932

2840280

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