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Information on EC 4.2.1.25 - L-Arabinonate dehydratase and Organism(s) Azospirillum brasilense and UniProt Accession Q1JUQ1

for references in articles please use BRENDA:EC4.2.1.25
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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.25 L-Arabinonate dehydratase
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This record set is specific for:
Azospirillum brasilense
UNIPROT: Q1JUQ1 not found.
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Word Map
The taxonomic range for the selected organisms is: Azospirillum brasilense
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
l-arabinonate dehydratase, l-arabonate dehydratase, rlardht, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-Arabonate dehydratase
-
Dehydratase, L-arabinonate
-
-
-
-
L-Arabonate dehydrase
-
-
-
-
L-Arabonate dehydratase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
L-arabinonate hydro-lyase (2-dehydro-3-deoxy-L-arabinonate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9024-30-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Arabinonate
2-Dehydro-3-deoxy-L-arabinonate
show the reaction diagram
-
-
-
?
L-Arabinonate
2-Dehydro-3-deoxy-L-arabinonate
show the reaction diagram
-
-
-
?
L-Arabinonate
?
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Arabinonate
?
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
the enzyme contains a [4Fe-4S]2+ cluster
Mg2+
optimal concentration: 1-10 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 29145
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ARADA_AZOBR
583
0
62252
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
128000
gel filtration
62000
2 * 62000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 62000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C124A
non-colored inactive mutant enzyme, the UV visible absorption spectrum contained no characteristic element of [4Fe-4S]2+
C197A
non-colored inactive mutant enzyme, the UV visible absorption spectrum contained no characteristic element of [4Fe-4S]2+
C441A
brown-colored mutant is significantly active and UV-visible absorption spectrum is similar to those of the wild-type enzyme
C47A
brown-colored mutant is significantly active and UV-visible absorption spectrum is similar to those of the wild-type enzyme
C56A
inactive mutant partiall shares similar behavior to the wild-type in color and UV-visible absorption spectrum
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzymes C47A, C56A, C124A, C197A, and C441A overexpressed in Escherichia coli cells as a His6-tagged enzymes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Novick, N.J.; Tyler, M.E.
L-Arabinose metabolism in Azospirillum brasiliense
J. Bacteriol.
149
364-367
1982
Azospirillum brasilense
Manually annotated by BRENDA team
Watanabe, S.; Shimada, N.; Tajima, K.; Kodaki, T.; Makino, K.
Identification and Characterization of L-Arabonate Dehydratase, L-2-Keto-3-deoxyarabonate Dehydratase, and L-Arabinolactonase Involved in an Alternative Pathway of L-Arabinose Metabolism: Novel Evolution ary Insight into Sugar Metabolism
J. Biol. Chem.
281
33521-33536
2006
Azospirillum brasilense (Q1JUQ1), Azospirillum brasilense
Manually annotated by BRENDA team