Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 5.5.1.27 - D-galactarolactone cycloisomerase and Organism(s) Agrobacterium fabrum and UniProt Accession A9CEQ7

for references in articles please use BRENDA:EC5.5.1.27
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme, characterized from the bacterium Agrobacterium fabrum strain C58, is involved in degradation of D-galacturonate and D-glucuronate. Activity with D-galactaro-1,4-lactone is 4-fold higher than with D-glucaro-1,4-lactone.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Agrobacterium fabrum
UNIPROT: A9CEQ7
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
  • 5.5.1.27
  • inappropriate
  • antidiuretic
  • osmolality
  • siadh
  • vasopressin
  • insipidus
  • hyponatremia
  • aldosterone
  • allozyme
  • toad
  • aldhs
  • renin
  • transepithelial
  • diuresis
  • hypertonic
  • hawaiian
  • brattleboro
  • obscura
  • 1.1.1.1
  • subgenus
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
galactarolactone cycloisomerase, more
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
D-galactaro-1,4-lactone lyase (ring-opening)
The enzyme, characterized from the bacterium Agrobacterium fabrum strain C58, is involved in degradation of D-galacturonate and D-glucuronate. Activity with D-galactaro-1,4-lactone is 4-fold higher than with D-glucaro-1,4-lactone.