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Information on EC 4.3.1.9 - glucosaminate ammonia-lyase and Organism(s) Pseudomonas fluorescens and UniProt Accession Q93HX6

for references in articles please use BRENDA:EC4.3.1.9
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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.9 glucosaminate ammonia-lyase
IUBMB Comments
Contains pyridoxal phosphate. The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes spontaneous hydrolytic deamination to form the final product.
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This record set is specific for:
Pseudomonas fluorescens
UNIPROT: Q93HX6
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The taxonomic range for the selected organisms is: Pseudomonas fluorescens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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Synonyms
ammonia-lyase, glucosaminate, D-glucosaminate dehydrogenase, D-glucosaminic acid dehydrase, EC 4.2.1.26, EC 4.3.1.21, GADH, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-glucosaminate dehydrogenase
-
EC 4.2.1.26
formerly
EC 4.3.1.21
formerly
ammonia-lyase, glucosaminate
-
-
-
-
D-glucosaminic acid dehydrase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
D-glucosaminate ammonia-lyase (isomerizing; 2-dehydro-3-deoxy-D-gluconate-forming)
Contains pyridoxal phosphate. The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes spontaneous hydrolytic deamination to form the final product.
CAS REGISTRY NUMBER
COMMENTARY hide
37290-91-8
-
9032-93-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glucosaminate
2-dehydro-3-deoxy-D-gluconate + NH3
show the reaction diagram
alpha,beta-elimination reaction
-
?
D-glucosaminate
pyruvate + glyceraldehyde + NH3
show the reaction diagram
aldolase reaction
-
?
thioredoxin + NADP+
? + NADPH
show the reaction diagram
alpha2 homodimer also has thioredoxin reductase activity
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0113
D-glucosaminic acid
pH 8
0.0113
pyridoxal 5'-phosphate
pH 8
0.0044
thioredoxin
pH 8
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GLCAL_PSEFL
320
0
33907
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33900
2 * 33900, alpha2-homodimer, SDS-PAGE
35000
2 * 35000, alpha,beta-heterodimer, SDS-PAGE
45000
2 * 45000, beta2-homodimer, SDS-PAGE
70000
alpha2-homodimer, SDS-PAGE
80000
alphabeta-heterodimer, SDS-PAGE
90000
beta2-homodimer, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Iwamoto, R.; Amano, C.; Ikehara, K.; Ushida, N.
The D-glucosaminate dehydratase alpha-subunit from Pseudomonas fluorescens exhibits thioredoxin reductase activity
Biochim. Biophys. Acta
1647
310-314
2003
Pseudomonas fluorescens (Q93HX6)
Manually annotated by BRENDA team