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

BRENDA support

BRENDA Home
show all | hide all No of entries

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

for references in articles please use BRENDA:EC4.3.1.18
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pseudomonas aeruginosa
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
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-serine dehydrase, d-ser dehydratase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-Hydroxy amino acid dehydratase
-
-
-
-
D-Serine deaminase
-
-
-
-
D-Serine dehydrase
-
-
-
-
D-Serine hydrolase (deaminating)
-
-
-
-
Dehydratase, D-serine
-
-
-
-
DSD
-
-
-
-
Dsdase
-
-
-
-
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
-
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
-
-
-
?
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A2C9WWJ0_PSEAI
448
0
48249
TrEMBL
-
A0A8G5JHV0_PSEAI
448
0
48258
TrEMBL
-
A0A8G2RD31_PSEAI
448
0
48095
TrEMBL
-
A0A8F9NWZ3_PSEAI
448
0
48169
TrEMBL
-
A0A8G5QVM8_PSEAI
448
0
48123
TrEMBL
-
A0A8G3EFX3_PSEAI
448
0
48245
TrEMBL
-
A0A0A8RG86_PSEAI
580
0
62658
TrEMBL
-
A0A5K1SEY3_PSEAI
448
0
48215
TrEMBL
-
A0A8G7MQ23_PSEAI
448
0
48245
TrEMBL
-
A0A8G5C9G6_PSEAI
448
0
48216
TrEMBL
-
A0A8G3B0L6_PSEAI
448
0
48263
TrEMBL
-
A0A8G2UF88_PSEAI
448
0
48233
TrEMBL
-
A0A3S0S2E9_PSEAI
448
0
48133
TrEMBL
-
A0A8G3XJ76_PSEAI
448
0
48214
TrEMBL
-
A0A8G2S3Z9_PSEAI
448
0
48229
TrEMBL
-
A0A8G7HGV7_PSEAI
448
0
48230
TrEMBL
-
A0A8G1K8A1_PSEAI
448
0
48187
TrEMBL
-
A0A659BPW4_PSEAI
448
0
48133
TrEMBL
-
A0A8G6FBM0_PSEAI
448
0
48231
TrEMBL
-
A0A444LXV5_PSEAI
448
0
48180
TrEMBL
-
A0A4P0UAX1_PSEAI
322
0
34659
TrEMBL
-
A0A0F6RQX5_PSEAI
448
0
48205
TrEMBL
-
A0A4U0J6W6_PSEAI
448
0
48185
TrEMBL
-
A0A7M3AX44_PSEAI
448
0
48184
TrEMBL
-
A0A8G2KEL6_PSEAI
448
0
48201
TrEMBL
-
A0A8G3JQ82_PSEAI
448
0
48219
TrEMBL
-
A0A8G4AGQ1_PSEAI
448
0
48185
TrEMBL
-
A0A8G6WLB9_PSEAI
448
0
48123
TrEMBL
-
A0A8G7LDD6_PSEAI
448
0
48168
TrEMBL
-
A0A2R4KQJ5_PSEAI
448
0
48233
TrEMBL
-
A0A8G7TD84_PSEAI
448
0
48245
TrEMBL
-
A0A8G2ZB29_PSEAI
448
0
48174
TrEMBL
-
A0A8F9VLE2_PSEAI
448
0
48165
TrEMBL
-
A0A8G4GA01_PSEAI
448
0
48245
TrEMBL
-
A0A367MH28_PSEAI
448
0
48229
TrEMBL
-
A0A8G6KDI7_PSEAI
448
0
48095
TrEMBL
-
A0A8G7MD85_PSEAI
448
0
48157
TrEMBL
-
A0A8G7ENQ1_PSEAI
448
0
48185
TrEMBL
-
A0A8G2VIT7_PSEAI
448
0
48190
TrEMBL
-
A0A4P0UC57_PSEAI
125
0
13380
TrEMBL
-
A0A5E8W3E8_PSEAI
448
0
48193
TrEMBL
-
A0A8G3IKJ4_PSEAI
448
0
48229
TrEMBL
-
A0A2R3IZF6_PSEAI
448
0
48162
TrEMBL
-
A0A8G2QJ42_PSEAI
448
0
48198
TrEMBL
-
A0A8G3K496_PSEAI
448
0
48201
TrEMBL
-
A0A8E5XLT5_PSEAI
448
0
48229
TrEMBL
-
A0A8G7DE44_PSEAI
448
0
48182
TrEMBL
-
A0A485FMT2_PSEAI
231
0
24925
TrEMBL
-
A0A8G7HTI2_PSEAI
448
0
48199
TrEMBL
-
A0A8B5BDS2_PSEAI
448
0
48245
TrEMBL
-
A0A643IRW8_PSEAI
396
0
42800
TrEMBL
-
A0A8G6AA12_PSEAI
448
0
48198
TrEMBL
-
A0A8G6XFK0_PSEAI
448
0
48054
TrEMBL
-
A0A8G2QK68_PSEAI
448
0
48259
TrEMBL
-
A0A6A9K468_PSEAI
448
0
48254
TrEMBL
-
A0A5F1BRZ7_PSEAI
448
0
48278
TrEMBL
-
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