Literature summary for 1.11.1.18 extracted from

Weyand, M.; Hecht, H.; Kiess, M.; Liaud, M.; Vilter, H.; Schomburg, D.
X-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 A resolution (1999), J. Mol. Biol., 293, 595-611.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of the enzyme is solved by single isomorphous replacement anomalous scattering X-ray crystallography at 2.0 A resolution. Crystals of the holoenzyme and the apoenzyme are obtained from 2.1 M ammonium sulfate solutions buffered at pH 8.3 and diffract to 2.4 A resolution. The crystals are stable in the X-ray beam for more than one week. They belong to the tetragonal system, space group P4(3)2(1)2, with lattice constants a ?= 114.3 A,? c = 276.0 A	Ascophyllum nodosum

Crystallization (Comment)

Organism

structure of the enzyme is solved by single isomorphous replacement anomalous scattering X-ray crystallography at 2.0 A resolution. Crystals of the holoenzyme and the apoenzyme are obtained from 2.1 M ammonium sulfate solutions buffered at pH 8.3 and diffract to 2.4 A resolution. The crystals are stable in the X-ray beam for more than one week. They belong to the tetragonal system, space group P4(3)2(1)2, with lattice constants a ?= 114.3 A,? c = 276.0 A

Ascophyllum nodosum

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Vanadium	the holoenzyme contains trigonal-bipyramidal coordinated vanadium atoms at its two active centres	Ascophyllum nodosum

Organism

Organism	UniProt	Comment	Textmining
Ascophyllum nodosum	P81701	-	-

Synonyms

Synonyms	Comment	Organism
V-BPO	-	Ascophyllum nodosum
vanadium-dependent haloperoxidase	-	Ascophyllum nodosum

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Release 2023.1 (January 2023)