Hydrolytic catalysis and structural stabilization in a designed metalloprotein (Q27676854)

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Language	Label	Description	Also known as
English	Hydrolytic catalysis and structural stabilization in a designed metalloprotein	scientific article

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instance of

scholarly article

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title

Hydrolytic catalysis and structural stabilization in a designed metalloprotein (English)

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author name string

Melissa L Zastrow

series ordinal

1

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Anna F A Peacock

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2

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Jeanne A Stuckey

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3

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Vincent L Pecoraro

series ordinal

4

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language of work or name

English

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inferred from title

publication date

27 November 2011

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published in

Nature Chemistry

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volume

4

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issue

2

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page(s)

118-23

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cites work

Switching the Chirality of the Metal Environment Alters the Coordination Mode in Designed Peptides

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Identifying important structural characteristics of arsenic resistance proteins by using designed three-stranded coiled coils

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Structural and functional importance of a conserved hydrogen bond network in human carbonic anhydrase II

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First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases

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Designing artificial enzymes by intuition and computation

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Design of functional metalloproteins

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Using diastereopeptides to control metal ion coordination in proteins

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Heterochromia in designed metallopeptides: geometry-selective binding of CdII in a de novo peptide

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Directed evolution of the promiscuous esterase activity of carbonic anhydrase II.

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De novo design of catalytic proteins

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Enzyme-like proteins by computational design

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De novo design and structural characterization of proteins and metalloproteins

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A designed metal-binding protein with a novel fold

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Grafting of a high-affinity Zn(II)-binding site on the beta-barrel of retinol-binding protein results in enhanced folding stability and enables simplified purification

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Scorpion toxins as natural scaffolds for protein engineering

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Models for metal ion function in carbonic anhydrase

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Disruption of the active site solvent network in carbonic anhydrase II decreases the efficiency of proton transfer.

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Thermodynamic model for the stabilization of trigonal thiolato mercury(II) in designed three-stranded coiled coils

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Binding of Cu(II) or Zn(II) in a de novo designed triple-stranded alpha-helical coiled-coil toward a prototype for a metalloenzyme

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Investigations of the esterase, phosphatase, and sulfatase activities of the cytosolic mammalian carbonic anhydrase isoforms I, II, and XIII with 4-nitrophenyl esters as substrates

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Kinetic study of catalytic CO(2) hydration by water-soluble model compound of carbonic anhydrase and anion inhibition effect on CO(2) hydration

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Peptidic models for the binding of Pb(II), Bi(III) and Cd(II) to mononuclear thiolate binding sites

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Esterase activities of human carbonic anhydrases B and C

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Reactive-site design in folded-polypeptide catalysts--the leaving group pKa of reactive esters sets the stage for cooperativity in nucleophilic and general-acid catalysis

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Carboxy and Phosphate Esters Cleavage with Mono- and Dinuclear Zinc(II) Macrocyclic Complexes in Aqueous Solution. Crystal Structure of [Zn(2)L1(&mgr;-PP)(2)(MeOH)(2)](ClO(4))(2) (L1 = [30]aneN(6)O(4), PP(-) = Diphenyl Phosphate)

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reference URL

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based on heuristic

inferred from PubMed ID database lookup

Importance of the conserved active-site residues Tyr7, Glu106 and Thr199 for the catalytic function of human carbonic anhydrase II

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/22270627

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1038/NCHEM.1201

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Dimensions Publication ID

1024698889

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PMC publication ID

3270697

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PubMed publication ID

22270627

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ResearchGate publication ID

221771247

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