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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.3.3.6 - pyridoxal 5'-phosphate synthase (glutamine hydrolysing) and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q03148

for references in articles please use BRENDA:EC4.3.3.6
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
             4.3.3 Amine-lyases
                4.3.3.6 pyridoxal 5'-phosphate synthase (glutamine hydrolysing)
IUBMB Comments
The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 A tunnel. The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate. The enzyme complex is found in aerobic bacteria, archaea, fungi and plants.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q03148
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: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
plp synthase, rv2606c, pyridoxal biosynthesis lyase, ph1355, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pyridoxal 5-phosphate synthase Snz1
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
D-ribose 5-phosphate,D-glyceraldehyde 3-phosphate pyridoxal 5'-phosphate-lyase
The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 A tunnel. The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate. The enzyme complex is found in aerobic bacteria, archaea, fungi and plants.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ribulose 5-phosphate + glyceraldehyde 3-phosphate + NH4+
pyridoxal 5'-phosphate + 4 H2O + phosphate
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion method, 16°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E116A
activity as the wild-type protein
K117A
no synthesis of pyridoxal 5'-phosphate, capacity to catalyse dihydroxyacetone phosphate isomerization
K148A
no synthesis of pyridoxal 5'-phosphate, capacity to catalyse dihydroxyacetone phosphate isomerization
K240A
activity as the wild-type protein
R136A/R137A
no synthesis of pyridoxal 5'-phosphate, dihydroxyacetone phosphate isomerization activity as the wild-type protein
R164A
completely inactive, dihydroxyacetone phosphate isomerization activity as the wild-type protein
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+), gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged protein expressed in Escherichia coli BL21 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, X.; Teng, Y.; Liu, J.; He, Y.; Zhou, K.; Chen, Y.; Zhou, C.
Structural insights into the catalytic mechanism of the yeast pyridoxal 5-phosphate synthase Snz1
Biochem. J.
432
445-450
2010
Saccharomyces cerevisiae (Q03148), Saccharomyces cerevisiae
Manually annotated by BRENDA team