About: Heterologous Expression of the Vanadium-containing Chloroperoxidase fromCurvularia inaequalisinSaccharomyces cerevisiaeand Site-directed Mutagenesis of the Active Site Residues His496, Lys353, Arg360, and Arg490

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About: Heterologous Expression of the Vanadium-containing Chloroperoxidase fromCurvularia inaequalisinSaccharomyces cerevisiaeand Site-directed Mutagenesis of the Active Site Residues His496, Lys353, Arg360, and Arg490 Goto Sponge NotDistinct Permalink

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scientific article published in Journal of Biological Chemistry

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в серпні 1999 (uk) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im August 1999 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q61679389-A8EBAFBF-542D-44B9-83B4-24839DF10ED6
publication date	1999-08-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q61679389-7B75ED8B-C76F-4C8D-80D1-7556E07FBCD7
language of work or name	English
author name string	wds:Q61679389-09047631-C505-4A7D-A672-B946B6E65D3B wds:Q61679389-330FDC5B-073E-4192-B19F-F449AE3F872D wds:Q61679389-7E6923B7-7705-47E5-8462-8CD09081EDEF wds:Q61679389-8706DDB2-BB06-4A39-BA4C-6AF3A35F9150
author name string	A Messerschmidt R Wever R Renirie W Hemrika
rdfs:label	Heterologous Expression of the Vanadium-containing Chloroperoxidase fromCurvularia inaequalisinSaccharomyces cerevisiaeand Site-directed Mutagenesis of the Active Site Residues His496, Lys353, Arg360, and Arg490 (en) Heterologous Expression of the Vanadium-containing Chloroperoxidase fromCurvularia inaequalisinSaccharomyces cerevisiaeand Site-directed Mutagenesis of the Active Site Residues His496, Lys353, Arg360, and Arg490 (nl)
skos:prefLabel	Heterologous Expression of the Vanadium-containing Chloroperoxidase fromCurvularia inaequalisinSaccharomyces cerevisiaeand Site-directed Mutagenesis of the Active Site Residues His496, Lys353, Arg360, and Arg490 (en) Heterologous Expression of the Vanadium-containing Chloroperoxidase fromCurvularia inaequalisinSaccharomyces cerevisiaeand Site-directed Mutagenesis of the Active Site Residues His496, Lys353, Arg360, and Arg490 (nl)
name	Heterologous Expression of the Vanadium-containing Chloroperoxidase fromCurvularia inaequalisinSaccharomyces cerevisiaeand Site-directed Mutagenesis of the Active Site Residues His496, Lys353, Arg360, and Arg490 (en) Heterologous Expression of the Vanadium-containing Chloroperoxidase fromCurvularia inaequalisinSaccharomyces cerevisiaeand Site-directed Mutagenesis of the Active Site Residues His496, Lys353, Arg360, and Arg490 (nl)
author	wds:Q61679389-68A1A520-D19C-41C5-B167-1CA3BF8B9FD8
author	Sandra Macedo-Ribeiro
title	wds:Q61679389-340836F8-6387-461A-B687-AAED764812E4
title	Heterologous expression of the vanadium-containing chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and site-directed mutagenesis of the active site residues His(496), Lys(353), Arg(360), and Arg(490) (en)
page(s)	wds:Q61679389-2E16ED52-C865-4760-9716-9C182309FC8A
page(s)	23820-23827
instance of	wds:Q61679389-3A65D6A5-CDB7-41A1-9CCF-1B0E363D496B
instance of	scholarly article
main subject	wds:Q61679389-EA3E2AAF-1D23-4190-B2E6-24F2B654CCC4
main subject	vanadium
PubMed ID	wds:Q61679389-CC37BF30-848D-4C06-B9C1-55D41CA46D3B
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10446144
PubMed ID	10446144
published in	wds:Q61679389-36EB9885-CD3F-4C1C-993E-F64E3E8B26F4
published in	Journal of Biological Chemistry
issue	wds:Q61679389-754539BE-A466-4C14-A629-7E65F435F600
volume	wds:Q61679389-A4E4B34E-F57C-425A-B1BA-05B36967E702
issue	34
volume	274
DOI	wds:Q61679389-DCF802C1-93ED-4CEC-874C-AF2BE21AF293
DOI	http://dx.doi.org/10.1074/JBC.274.34.23820
DOI	10.1074/JBC.274.34.23820
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q61679389
is cites work of	A stereoselective vanadium-dependent chloroperoxidase in bacterial antibiotic biosynthesis Mechanistic considerations of halogenating enzymes The unique biogeochemical signature of the marine diazotroph trichodesmium Exploring the chemistry and biology of vanadium-dependent haloperoxidases Complexation of oxoanions and cationic metals by the biscatecholate siderophore azotochelin Vanadium-dependent iodoperoxidases in Laminaria digitata, a novel biochemical function diverging from brown algal bromoperoxidases The catalytic center of glucose-6-phosphatase. HIS176 is the nucleophile forming the phosphohistidine-enzyme intermediate during catalysis The Vanadium Iodoperoxidase from the marine flavobacteriaceae species Zobellia galactanivorans reveals novel molecular and evolutionary features of halide specificity in the vanadium haloperoxidase enzyme family. Modification of halogen specificity of a vanadium-dependent bromoperoxidase Enzymatic Halogenation and Dehalogenation Reactions: Pervasive and Mechanistically Diverse Selective oxidative decarboxylation of amino acids to produce industrially relevant nitriles by vanadium chloroperoxidase Bromoperoxidase activity of vanadate-substituted acid phosphatases from Shigella flexneri and Salmonella enterica ser. typhimurium. Sulfoxidation mechanism of vanadium bromoperoxidase from Ascophyllum nodosum. Evidence for direct oxygen transfer catalysis Reactivity of recombinant and mutant vanadium bromoperoxidase from the red alga Corallina officinalis. N-Salicylidenehydrazides as versatile tridentate ligands for dioxovanadium(V) complexes Towards models of vanadate-dependent haloperoxidases: the hydroxyl side chain Moraxella catarrhalis synthesizes an autotransporter that is an acid phosphatase. Characterizing the complexity of enzymes on the basis of their mechanisms and structures with a bio-computational analysis. Oxidation reactions catalyzed by vanadium chloroperoxidase from Curvularia inaequalis. An Ultrasensitive Fluorescence Assay for the Detection of Halides and Enzymatic Dehalogenation
is cites work of	wds:Q28730333-64EA9F90-39EE-4B11-A0C2-C38F9E69B8FA wds:Q50109872-DAE75EB5-DBC9-4845-94C1-1BCEA91820B3 wds:Q73966792-1B3F5B8B-4FE6-4574-9B6B-1B3F1BCBBB07 wds:Q84067972-B01E819B-F259-4BC1-AB89-470A5C05D3F0 wds:Q34731119-7E97EB37-70BC-432B-825A-C5401B2C2CF6 wds:Q37579055-C886BCDD-2779-4200-851E-9034A64E5FD7 wds:Q73966797-E0B3AB43-FCC9-454C-BEF3-863DA3CAC635 wds:Q38768051-0D075242-A025-49A8-A805-DB32F3C9EC6F wds:Q79435209-1B107FC9-099C-4CC6-AB74-7F69A9055E51 wds:Q37878575-A38CB455-A08C-46DC-A11B-C0A6946BF6C7 wds:Q44066708-D4A62FEF-85F4-4DCF-9FEF-D351E5E65FAF wds:Q33928471-A2C2E82B-DBD4-4569-A9F8-BEC8FCEC16DB wds:Q34975328-C4610894-AC5E-4A1E-ADA0-5E6102807BE4 wds:Q34595589-0DBCBB4E-8402-48AA-8873-8EA64A809CF9 wds:Q24646368-7D8D51CD-F3A7-444C-B3EA-A7341EEB67D5 wds:Q24300780-2C03A367-9A7D-4851-9AC8-49CB2667FA08 wds:Q41996248-4B0E9ACF-1A2F-4060-ADB1-0B65CF8550E4 wds:Q50510886-3A7EC2F7-32E7-4B36-BEE2-EF530D3C4AA6 wds:Q63487430-B317DA8D-0EC4-40A9-B4A6-D39F75389764 wds:Q94503037-B1AA46D1-73AF-4B42-9D1D-A866983B817A

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