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Information on EC 3.5.4.44 - ectoine hydrolase and Organism(s) Halomonas elongata and UniProt Accession E1V7W1

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.4 In cyclic amidines
                3.5.4.44 ectoine hydrolase
IUBMB Comments
The enzyme, found in some halophilic bacteria, is involved in the degradation of the compatible solute ectoine. The enzyme, which belongs to peptidase family M24, only acts in the direction of ectoine hydrolysis. It also produces smaller amounts of (2S)-4-acetamido-2-aminobutanoate, which is recycled back to ectoine by EC 4.2.1.108, ectoine synthase.
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This record set is specific for:
Halomonas elongata
UNIPROT: E1V7W1
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The taxonomic range for the selected organisms is: Halomonas elongata
The enzyme appears in selected viruses and cellular organisms
Synonyms
ectoine hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
doeA
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ectoine aminohydrolase
The enzyme, found in some halophilic bacteria, is involved in the degradation of the compatible solute ectoine. The enzyme, which belongs to peptidase family M24, only acts in the direction of ectoine hydrolysis. It also produces smaller amounts of (2S)-4-acetamido-2-aminobutanoate, which is recycled back to ectoine by EC 4.2.1.108, ectoine synthase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ectoine + H2O
N2-acetyl-L-2,4-diaminobutanoate
show the reaction diagram
-
-
-
?
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the degradation of ectoine proceeds via hydrolysis of ectoine by DoeA to Nalpha-acetyl-L-2,4-diaminobutanoate, followed by deacetylation to diaminobutanoate by DoeB and a transaminase reaction by DoeD leading to aspartate-semialdehyde. Deletion of doeA results in a mutant that cannot utilize ectoine as carbon and nitrogen source
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 44900, calculated
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schwibbert, K.; Marin-Sanguino, A.; Bagyan, I.; Heidrich, G.; Lentzen, G.; Seitz, H.; Rampp, M.; Schuster, S.C.; Klenk, H.P.; Pfeiffer, F.; Oesterhelt, D.; Kunte, H.J.
A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581 T
Environ. Microbiol.
13
1973-1994
2011
Halomonas elongata (E1V7W1), Halomonas elongata DSM 2581 (E1V7W1)
Manually annotated by BRENDA team