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Information on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and Organism(s) Staphylococcus aureus and UniProt Accession Q6GIL8

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IUBMB Comments
Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
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This record set is specific for:
Staphylococcus aureus
UNIPROT: Q6GIL8
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The taxonomic range for the selected organisms is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
gapdhs, d-glyceraldehyde-3-phosphate dehydrogenase, gapds, gadph, glyceraldehyde-3-phosphate dehydrogenases, plasmin receptor, gapc1, plasminogen-binding protein, gapcp, glyceraldehyde-3 phosphate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glyceraldehyde-3-phosphate dehydrogenase 1
-
3-phosphoglyceraldehyde dehydrogenase
-
-
-
-
BARS-38
-
-
-
-
CP 17/CP 18
-
-
-
-
dehydrogenase, glyceraldehyde phosphate
-
-
-
-
dihydrogenase, glyceraldehyde phosphate
-
-
-
-
G3PD
-
-
-
-
GAPDH
-
-
-
-
GAPDH1
-
-
-
-
GAPDH2
-
-
-
-
glyceraldehyde phosphate dehydrogenase (NAD)
-
-
-
-
glyceraldehyde-3-P-dehydrogenase
-
-
-
-
glyceraldehyde-3-phosphate dehydrogenase (NAD)
-
-
-
-
GPD
-
-
-
-
Gra3PDH
-
-
-
-
GraP-DH
-
-
-
-
Larval antigen OVB95
-
-
-
-
Major larval surface antigen
-
-
-
-
NAD+-G-3-P dehydrogenase
-
-
-
-
NAD-dependent glyceraldehyde phosphate dehydrogenase
-
-
-
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NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
-
-
-
-
NAD-G3PDH
-
-
-
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NADH-glyceraldehyde phosphate dehydrogenase
-
-
-
-
P-37
-
-
-
-
phosphoglyceraldehyde dehydrogenase
-
-
-
-
Plasmin receptor
-
-
-
-
Plasminogen-binding protein
-
-
-
-
TLAb
-
-
-
-
triose phosphate dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating)
Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-50-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.31 - 0.34
D-glyceraldehyde 3-phosphate
312 - 322
NAD+
2.54 - 3.68
phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 70
D-glyceraldehyde 3-phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37500
x * 37600, calculated, x * 37500, SDS-PAGE
37600
x * 37600, calculated, x * 37500, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 37600, calculated, x * 37500, SDS-PAGE
homotetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M Tris-HCl pH 8.2, 28% (w/v) PEG 3350, at 25°C
to 2.0 A resolution. Space group P21
wild type holo and apoenzymes and mutant enzymes C151S, C151G and C151S/H178N in complex with NAD+ and D-glyceraldehyde 3-phosphate, hanging drop vapor diffusion method, the wild-type holoenzyme and apoenzyme are crystallized from 0.1 M Tris-HCl, pH 8.5, and 20% (w/v) PEG 4000 at 4°C and from 0.1 M Tris-HCl, pH 8.2, and 32% (w/v) PEG 3350 at 25°C, respectively. Crystals of active-site mutants in complex with NAD+ (C151S, C151G, and C151S/H178N) grow at 25°C from 0.1 M Tris-HCl, pH 8.5, and 28% (w/v) PEG 4000, from 0.1 M Tris-HCl, pH 8.2, and 30% (w/v) PEG 4000, and from 0.1 M Tris-HCl, pH 8.5, and 30% (w/v) PEG 4000, respectively, while mutant H178N in complex with NAD+ crystallizes from 0.1 M Tris-HCl, pH 8.2, and 30% (w/v) PEG 4000 at 4°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C151/H178N
the rate of the forward reaction is decreased by 47000 times compared to the wild type enzyme with similar affinity for the substrate and the coenzyme
C151G
the mutant is completely inactive
C151S
the mutant shows drastically reduced kcat values compared to the wild type enzyme
H178N
the mutant shows no significant difference in the Km values of D-glyceraldehyde 3-phosphate, phosphate, and NAD+ compared to the wild type enzyme, however, the mutation results in the reduction of kcat of oxidative phosphorylation by 1400times
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-Sepharose column chromatography and Superdex 75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli M15 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mukherjee, S.; Dutta, D.; Saha, B.; Das, A.K.
Expression, purification, crystallization and preliminary X-ray diffraction studies of glyceraldehyde-3-phosphate dehydrogenase 1 from methicillin-resistant Staphylococcus aureus (MRSA252)
Acta Crystallogr. Sect. F
64
929-932
2008
Staphylococcus aureus (Q6GIL8), Staphylococcus aureus, Staphylococcus aureus MRSA252 (Q6GIL8)
Manually annotated by BRENDA team
Mukherjee, S.; Saha, B.; Dutta, D.; Das, A.
Purification, crystallization and preliminary X-ray analysis of apo glyceraldehyde-3-phosphate dehydrogenase 1 (GAP1) from methicillin-resistant Staphylococcus aureus (MRSA252)
Acta Crystallogr. Sect. F
66
506-508
2010
Staphylococcus aureus (Q6GIL8), Staphylococcus aureus, Staphylococcus aureus MRSA252 (Q6GIL8)
Manually annotated by BRENDA team
Mukherjee, S.; Dutta, D.; Saha, B.; Das, A.K.
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase 1 from methicillin-resistant Staphylococcus aureus MRSA252 provides novel insights into substrate binding and catalytic mechanism
J. Mol. Biol.
401
949-968
2010
Staphylococcus aureus (Q6GIL8), Staphylococcus aureus, Staphylococcus aureus MRSA252 (Q6GIL8), Staphylococcus aureus MRSA252
Manually annotated by BRENDA team