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Literature summary for 4.2.1.43 extracted from

  • Shimada, N.; Mikami, B.; Watanabe, S.; Makino, K.
    Preliminary crystallographic analysis of L-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of L-arabinose metabolism (2007), Acta Crystallogr. Sect. F, 63, 393-395.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed as a N-terminal His6-tagged protein in Escherichia coli Azospirillum brasilense

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallized at 18°C using the hanging-drop vapour-diffusion method. The crystal diffracts to 2.0 A resolution using synchrotron radiation and belongs to the trigonal space group P3(1)2(1) or its enantiomorph P3(2)2(1), with unit-cell parameters a = b = 78.91, c = 207.71 A Azospirillum brasilense

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
2 * 35000, SDS-PAGE Azospirillum brasilense
85000
-
gel filtration Azospirillum brasilense

Organism

Organism UniProt Comment Textmining
Azospirillum brasilense Q1JUQ0
-
-

Subunits

Subunits Comment Organism
dimer 2 * 35000, SDS-PAGE Azospirillum brasilense

Synonyms

Synonyms Comment Organism
L-2-keto-3-deoxyarabonate dehydratase
-
Azospirillum brasilense
L-KDA dehydratase
-
Azospirillum brasilense