Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme
about
Crystal structure of HLA-DP2 and implications for chronic beryllium diseaseCharacterization of native and recombinant forms of an unusual cobalt-dependent proline dipeptidase (prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus.Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymesThe anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidaseMolecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2Interactions of Streptomyces griseus aminopeptidase with amino acid reaction products and their implications toward a catalytic mechanismCobalt substitution of mouse R2 ribonucleotide reductase as a model for the reactive diferrous state: spectroscopic and structural evidence for a ferromagnetically coupled dinuclear cobalt clusterInhibition of Monometalated Methionine Aminopeptidase: Inhibitor Discovery and Crystallographic Analysis †Structural and functional analysis of the Spt16p N-terminal domain reveals overlapping roles of yFACT subunitsStructural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymesStructure of a microsporidian methionine aminopeptidase type 2 complexed with fumagillin and TNP-470Organophosphorus acid anhydrolase fromAlteromonas macleodii: structural study and functional relationship to prolidasesCryo-EM structures of Arx1 and maturation factors Rei1 and Jjj1 bound to the 60S ribosomal subunitThe Structure of RdDddP from Roseobacter denitrificans Reveals That DMSP Lyases in the DddP-Family Are MetalloenzymesStructure and mechanism of a proline-specific aminopeptidase from Escherichia coliAmino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases.Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differencesAdvances in Bacterial Methionine Aminopeptidase InhibitionStructural trees for protein superfamilies.Cloning, expression, and characterization of tomato (Lycopersicon esculentum) aminopeptidase P.Cobalt proteins.Crystal Structural and Functional Analysis of the Putative Dipeptidase from Pyrococcus horikoshii OT3Amino acid residues involved in the functional integrity of Escherichia coli methionine aminopeptidase.[μ-(4S,5S,15S,16S)-10,21-Di-tert-butyl-4,5,15,16-tetra-phenyl-3,6,14,17-tetra-aza-tricyclo-[17.3.1.1]tetra-cosa-1(23),8,10,12(24),19,21-hexa-ene-23,24-diolato-κN,N,O,O:NN,O,O]bis-[(acetato-κO)zinc(II)] ethanol disolvate[μ-14,29-Di-tert-butyl-3,10,18,25-tetra-azatpenta-cyclo-[25.3.1.1.0.0]dotriaconta-1(31),4,6,8,12(32),14,16,19,21,23,27,29-dodeca-ene-31,32-diol-ato]bis-[(nitrato-κO,O')zinc(II)].Impact of the N-terminal amino acid on targeted protein degradation.Bacterial protease inhibitors.Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold.All in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly.Tuned by metals: the TET peptidase activity is controlled by 3 metal binding sites.A single amino acid residue defines the difference in ovalicin sensitivity between type I and II methionine aminopeptidasesEmerging trends in metalloprotein inhibition.TvMP50 is an immunogenic metalloproteinase during male trichomoniasisStructurally distinct active sites in the copper(II)-substituted aminopeptidases from Aeromonas proteolytica and Escherichia coliMutation of H63 and its catalytic affect on the methionine aminopeptidase from Escherichia coli.Analyzing the binding of Co(II)-specific inhibitors to the methionyl aminopeptidases from Escherichia coli and Pyrococcus furiosusAnalyzing the catalytic role of Asp97 in the methionine aminopeptidase from Escherichia coli.Kinetic and spectroscopic analysis of the catalytic role of H79 in the methionine aminopeptidase from Escherichia coli.The biological occurrence and trafficking of cobalt.Organophosphorus hydrolase as an in vivo catalytic nerve agent bioscavenger.
P2860
Q24305214-A06C7EC6-42F2-4C44-8F4B-B94D8C9E2116Q24521506-81926988-5EBD-4BC3-BFF8-2408CF76A1DDQ24561556-EF2E95A3-32DE-442A-9283-DBE2B1A2E690Q24646329-2BAA0B38-B4E5-4255-906F-A614560D27BAQ24651202-138CBD50-596A-4F82-A3D4-B766E645C711Q27633855-50140601-5480-4472-AF38-4980AF7E1B12Q27639266-6C5CA5EF-51A0-47C8-A73D-7E39957598E5Q27648848-E4B6D1BC-63D5-4FA6-BCB0-9A9334F380B2Q27649362-365F8B50-C7D5-482A-A4F1-FE28FB4F6AEDQ27649367-414FA961-1A0A-4D90-A507-D3C7CF6DA1D4Q27656912-5B8AB431-2FD2-44F2-B884-ABCD25A26941Q27677152-C58CB21C-FE24-47DC-9A4E-0D79F08DB3B5Q27683374-AD44DFF0-1D92-48DD-8BC0-FD5F68BAF01AQ27684797-C0246FEA-F027-4F78-984C-D836E8B7F9A4Q27748986-41CE244B-5AC2-4D08-9520-054AEE71E351Q27936010-BDDA020F-BF1F-49A2-AF1E-619BC195C940Q28201642-3979ABFB-8DAE-4AA4-943C-546EBB60D83BQ28831446-E47A3F7F-FFCB-4DE8-8D38-3253DD6FB614Q30427554-ADB40BA5-E588-436A-9AED-410EAEA5AB30Q30681385-E19651FB-F9B1-4E27-9BCA-4A3276CD2A51Q33548215-6AF6AED9-373A-46A2-A06E-A546C491979DQ33621760-EB8BCC12-9886-484E-912A-5EB5259B7741Q33635634-A05F44D0-8A77-47E6-9725-B5BD84DF8BEAQ34264622-5419B4CD-2929-4B2B-A402-368DC4C59D81Q34294369-2CB4ED4C-B399-47FE-9663-34BFE67911F9Q34557941-6D2DDB16-8D62-42A7-93B0-255D40765EF6Q34732982-D033C403-ECFD-4EFC-ABC8-6A9672E637ACQ35116530-4FF51940-18FA-4796-9275-655166076717Q36281126-D8ABE29E-10AC-4B3D-913C-31C71CBE45FFQ36555459-7C403C91-C4A3-4167-8598-9794B4CDE598Q36915728-20B5BD28-C3C9-409A-9FCD-027C30F9417BQ36956841-35215E76-2853-4B49-9226-BDC06804CDF2Q37001987-426C5A36-5410-4213-A0DF-F3B65DD9B69DQ37160016-67C24C65-D970-47B8-B431-5684C62825BAQ37172110-13CB211E-E7C9-4032-879A-8520BF6EAD30Q37182391-4287C3F6-C273-4E85-BCF5-8E5E5C6463BDQ37234265-A3E2485B-91D2-407F-888D-EF2EE12DC2CBQ37289154-25B5DCBC-2CA9-46FA-9310-8BCDDA53213AQ37909062-F1BCD2E0-36F1-444E-817E-50B8F0C971E9Q37989116-39BAA72A-44D2-4EA7-B29D-234B56D6E49A
P2860
Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme
description
1993 nî lūn-bûn
@nan
1993 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Structure of the cobalt-depend ...... new type of proteolytic enzyme
@ast
Structure of the cobalt-depend ...... new type of proteolytic enzyme
@en
Structure of the cobalt-depend ...... new type of proteolytic enzyme
@nl
type
label
Structure of the cobalt-depend ...... new type of proteolytic enzyme
@ast
Structure of the cobalt-depend ...... new type of proteolytic enzyme
@en
Structure of the cobalt-depend ...... new type of proteolytic enzyme
@nl
prefLabel
Structure of the cobalt-depend ...... new type of proteolytic enzyme
@ast
Structure of the cobalt-depend ...... new type of proteolytic enzyme
@en
Structure of the cobalt-depend ...... new type of proteolytic enzyme
@nl
P921
P356
P1433
P1476
Structure of the cobalt-depend ...... new type of proteolytic enzyme
@en
P2093
B W Matthews
S L Roderick
P304
P356
10.1021/BI00066A009
P407
P577
1993-04-20T00:00:00Z