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Information on EC 4.3.1.18 - D-Serine ammonia-lyase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HYN9

for references in articles please use BRENDA:EC4.3.1.18
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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.18 D-Serine ammonia-lyase
IUBMB Comments
A pyridoxal-phosphate protein. The enzyme cleaves a carbon-oxygen bond, releasing a water molecule (hence the enzyme's original classification as EC 4.2.1.14, D-serine dehydratase) and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also acts, slowly, on D-threonine.
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This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: Q9HYN9
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
d-serine dehydratase, d-serine deaminase, dsdase, dsd1p, d-serine ammonia lyase, dsdsc, d-serine ammonia-lyase, d-ser dehydratase, d-serine dehydrase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-Hydroxy amino acid dehydratase
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D-Serine deaminase
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D-Serine dehydrase
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D-Serine hydrolase (deaminating)
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Dehydratase, D-serine
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DSD
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Dsdase
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SYSTEMATIC NAME
IUBMB Comments
D-serine ammonia-lyase (pyruvate-forming)
A pyridoxal-phosphate protein. The enzyme cleaves a carbon-oxygen bond, releasing a water molecule (hence the enzyme's original classification as EC 4.2.1.14, D-serine dehydratase) and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also acts, slowly, on D-threonine.
CAS REGISTRY NUMBER
COMMENTARY hide
9015-88-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-serine
pyruvate + NH3
show the reaction diagram
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-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.33
D-serine
pH and temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PAO1
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
due to its low level of expression and the lack of induction by exogenous D-serine, this dsdA gene does not have any apparent contribution to D-serine utilization in Pseudomonas aeruginosa PAO1. However, a high level of DsdA when overexpressed from a recombinant plasmid is able to support growth on D-serine as the sole source of carbon and nitrogen
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
no induction by exogenous D-serine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, G.; Lu, C.D.
The cryptic dsdA gene encodes a functional D-serine dehydratase in Pseudomonas aeruginosa PAO1
Curr. Microbiol.
72
788-794
2016
Pseudomonas aeruginosa (Q9HYN9), Pseudomonas aeruginosa
Manually annotated by BRENDA team