Investigation of the roles of catalytic residues in serotonin N-acetyltransferase - Wikidata - awgldk - TriplyDB

Investigation of the roles of catalytic residues in serotonin N-acetyltransferase

Investigation of the roles of catalytic residues in serotonin N-acetyltransferase

http://www.wikidata.org/entity/Q27638256

about

Crystal structures of murine carnitine acetyltransferase in ternary complexes with its substrates De novo discovery of serotonin N-acetyltransferase inhibitors Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT)The molecular basis of glyphosate resistance by an optimized microbial acetyltransferase Mechanistic and Structural Analysis of Aminoglycoside N -Acetyltransferase AAC(6′)-Ib and Its Bifunctional, Fluoroquinolone-Active AAC(6′)-Ib-cr Variant † ‡Structure and Biochemical Characterization of Protein Acetyltransferase from Sulfolobus solfataricus Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production Evolution of insect arylalkylamine N-acetyltransferases: Structural evidence from the yellow fever mosquito, Aedes aegypti Crystal structure of the dopamine N -acetyltransferase–acetyl-CoA complex provides insights into the catalytic mechanism Three-dimensional structure of aStreptomyces sviceusGNAT acetyltransferase with similarity to the C-terminal domain of the human GH84O-GlcNAcase Structural insights into WcbI, a novel polysaccharide-biosynthesis enzyme An intramolecular disulfide bridge as a catalytic switch for serotonin N-acetyltransferase Mechanistic analysis of Mycobacterium tuberculosis Rv1347c, a lysine Nepsilon-acyltransferase involved in mycobactin biosynthesis On the role of residue phosphorylation in 14-3-3 partners: AANAT as a case study.Evolution of AANAT: expansion of the gene family in the cephalochordate amphioxus Crystal structure of TDP-fucosamine acetyltransferase (WecD) from Escherichia coli, an enzyme required for enterobacterial common antigen synthesis.Mechanistic and structural analysis of Drosophila melanogaster arylalkylamine N-acetyltransferases.in-silico study of arylalkylamine-nacetyltransferase enzyme to regulate circadian rhythmicity Molecular evolution of multiple arylalkylamine N-acetyltransferase (AANAT) in fish.Crystal structure of Helicobacter pylori pseudaminic acid biosynthesis N-acetyltransferase PseH: implications for substrate specificity and catalysis.Probing the chemical mechanism and critical regulatory amino acid residues of Drosophila melanogaster arylalkylamine N-acyltransferase like 2 Molecular Evolution of Aralkylamine N-Acetyltransferase in Fish: A Genomic Survey.Mechanistic and Structural Analysis of a Drosophila melanogaster Enzyme, Arylalkylamine N-Acetyltransferase Like 7, an Enzyme That Catalyzes the Formation of N-Acetylarylalkylamides and N-Acetylhistamine.Evidence that proline focuses movement of the floppy loop of arylalkylamine N-acetyltransferase (EC 2.3.1.87).Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function The molecular basis of the expansive substrate specificity of the antibiotic resistance enzyme aminoglycoside acetyltransferase-6'-aminoglycoside phosphotransferase-2". The role of ASP-99 as an active site base important for acetyl transfer.Homology modeling and prediction of the amino acid residues participating in the transfer of acetyl-CoA to arylalkylamine by the N-acetyltransferase from Chryseobacterium sp.Functional diversity of Teleost arylalkylamine N-acetyltransferase-2: is the timezyme evolution driven by habitat temperature?Investigation of the catalytic triad of arylamine N-acetyltransferases: essential residues required for acetyl transfer to arylamines.Structural and Mechanistic Analysis of Drosophila melanogaster Agmatine N-Acetyltransferase, an Enzyme that Catalyzes the Formation of N-Acetylagmatine.The Mechanism of Acetyl Transfer Catalyzed by Mycobacterium tuberculosis GlmU.

P2860

Q24607519-AFE4F24E-FD1F-4636-9C7B-091BB063C874 Q24653710-45446BC5-99D9-40EC-A0F6-12E1A3594B6C Q26314426-A456C561-A814-4F62-8CF6-C5D00DE2A984 Q27643715-570CCC06-B4AC-4808-A172-6318EC8814DA Q27651667-1D3C3633-BD0D-41F5-9AA0-91AE26BDD581 Q27655636-B82A6137-C87A-45E2-9C6D-84FEFB1A5EEB Q27668134-21EC9BCA-4ACA-4E4D-9C71-048D6D0B3472 Q27670611-A67EF04C-0598-43C5-8454-CAF7E4C0E8BE Q27681264-16C17A37-1DAC-4EF4-AD26-AA97E57D6953 Q27681305-828F8139-6F6E-4B3F-834F-DD1AE52A65A4 Q27684860-C7BF809B-77D4-46DB-B6A0-9151C0AB0922 Q28221252-59D71E09-890F-49B0-B31E-69EFEE690690 Q28487185-73EB22C7-6A48-4F29-BA95-34F6C16C1D1B Q30844532-72C331EB-0DC6-4398-B24B-30817802B68B Q33586856-79D1DAAF-258E-4279-AFAE-E6DFFFFFE010 Q34549307-5F5D8C3F-9BB3-48AE-BE6D-D9CC9FA69A9A Q34731719-25351846-715C-4C7D-B4C1-45F5E312D072 Q34983444-B4860CBC-B9CF-48C9-A5E4-EB44EFE4B4ED Q35034693-4027A2B5-E807-4625-A621-C6E4420D28F7 Q35579784-FCEDA889-D6C0-4E74-8D3C-63B9DF261BC3 Q36328485-865E50AF-89F5-4A03-9EAF-D947B1A28BB5 Q36512492-34846578-DC44-40DA-88EB-F72BAB9FBC33 Q36567484-7571A5B0-76DE-409B-B235-05BACEBF2871 Q36662745-7BAE5663-A822-47E4-BBEB-3413E14E80A6 Q37290564-8766E6C5-C211-4060-B9A7-22557AC12950 Q38358019-7CB861D2-8A73-44BD-BBE5-8B1FF2262CE1 Q38672897-CC3E27FE-BA75-4CCC-8A7A-00C85EFEEB4E Q38935292-819A6EFC-E805-4263-91EC-FAF3E8E98EC0 Q41764388-E449CE4C-A478-422C-AB41-2537A30A79CE Q42677587-CA40B67B-30E8-47B9-8A6B-BAE7E2FFCBA6 Q52312613-EE95ED2E-8A34-42E4-A1CF-3F8B9E1445E8

P2860

Investigation of the roles of catalytic residues in serotonin N-acetyltransferase

http://www.wikidata.org/entity/Q27638256

description

2002 nî lūn-bûn

@nan

2002 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Investigation of the roles of catalytic residues in serotonin N-acetyltransferase

@ast

Investigation of the roles of catalytic residues in serotonin N-acetyltransferase

@en

Investigation of the roles of catalytic residues in serotonin N-acetyltransferase

@nl

type

label

Investigation of the roles of catalytic residues in serotonin N-acetyltransferase

@ast

Investigation of the roles of catalytic residues in serotonin N-acetyltransferase

@en

Investigation of the roles of catalytic residues in serotonin N-acetyltransferase

@nl

prefLabel

Investigation of the roles of catalytic residues in serotonin N-acetyltransferase

@ast

Investigation of the roles of catalytic residues in serotonin N-acetyltransferase

@en

Investigation of the roles of catalytic residues in serotonin N-acetyltransferase

@nl

P1433

Q27638256-C45EE103-CEB7-4D99-B055-E62C34F056A5

P1476

Q27638256-38AB9D3B-51FE-4288-BE5E-0E28E37C913D

P2093

Q27638256-2D064EC2-CF50-4F9D-9326-E454FC1F58D1

Q27638256-43D3E49B-42F5-444F-BE25-04FC4DE06EF6

Q27638256-C471C2D8-ED7D-4A0E-BF66-383BFC25061D

Q27638256-F1527D31-4123-46BD-85E1-227AFAD88586

P2860

Q27638256-0995AA64-1242-402E-936F-01D348DF736A

Q27638256-0AB6F9C3-8128-4217-AAB3-5120F9C4CDA2

Q27638256-27810695-90CC-46F6-B575-1CF930DCEB3D

Q27638256-3053E9E6-6D7B-48BA-9B0B-5AA693AFD9FD

Q27638256-3B83C827-2363-4F12-957C-67EE726CCA62

Q27638256-40BAABCB-D872-4238-8325-E6126F6DED63

Q27638256-40BCC149-4EA7-4335-97A6-2D09F253BA80

Q27638256-4BB87F89-D93A-4AA3-BA71-4F70B8CCFF86

Q27638256-5C8679DB-2C97-4AEE-8C03-71D853CFD188

Q27638256-5F028A65-0E84-40FF-A2FE-F4356D27455E

P304

Q27638256-3CE6B41B-DBF9-40BD-AF9B-D30F5FF9FB78

P31

Q27638256-9D09C492-818D-4F9E-A823-E058DB94E35B

P3181

Q27638256-69B03670-3091-4D40-8F0A-069195BAEBA2

P356

Q27638256-82729773-A3C3-4D1B-9D89-70BB670E8A0A

P407

Q27638256-7854D8C2-4A7C-4B62-98ED-0FD2E9EBDEE3

P433

Q27638256-A059DC7C-B525-4BAA-B07E-DD0540F8B68C

P478

Q27638256-9460AF6D-4E4C-46EB-880F-F1630F5481AE

P577

Q27638256-8684CCFE-B717-4931-8E5C-0CCCA199E24A

P5875

Q27638256-2E11392E-3A55-45FC-81DD-4A69F42A4E39

P698

Q27638256-66410B89-0505-49C9-A31A-8384A26CFEDD

P921

Q27638256-2f64f1cd-c1a3-472c-a998-06109cf8395c

P3181

P356

P1433

Journal of Biological Chemistry

P1476

Investigation of the roles of catalytic residues in serotonin N-acetyltransferase

@en

P2093

Jacqueline De Angelis

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

Kara A Scheibner

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

Philip A Cole

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

Stephen K Burley

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

P2860

Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation

Mechanism-based inhibition of the melatonin rhythm enzyme: pharmacologic exploitation of active site functional plasticity

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

PROCHECK: a program to check the stereochemical quality of protein structures

Processing of X-ray diffraction data collected in oscillation mode

The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog

Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide

X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate

X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition

P304

18118-26

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

P31

scholarly article

P3181

4731895

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

P356

10.1074/JBC.M200595200

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

P407

P433

20

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

P478

277

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

P577

2002-05-17T00:00:00Z

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

P5875

11479510

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

P698

11884405

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

P921