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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.7.92 - 3-deoxy-D-glycero-D-galacto-nonulopyranosonate cytidylyltransferase and Organism(s) Mus musculus and UniProt Accession Q99KK2

for references in articles please use BRENDA:EC2.7.7.92
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme is part of the biosynthesis pathway of the sialic acid 3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate (Kdn). Kdn is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mus musculus
UNIPROT: Q99KK2
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: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
cmp-kdn synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-deoxy-D-glycero-D-galacto-nononate cytidylyltransferase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
CTP:3-deoxy-D-glycero-D-galacto-nononate cytidylyltransferase
The enzyme is part of the biosynthesis pathway of the sialic acid 3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate (Kdn). Kdn is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CTP + 3-deoxy-D-glycero-D-galacto-nononate
diphosphate + CMP-3-deoxy-D-glycero-D-galacto-nononate
show the reaction diagram
-
-
-
?
CTP + N-acetylneuraminic acid
diphosphate + CMP-N-acetylneuraminic acid
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.56
3-deoxy-D-glycero-D-galacto-nononate
pH 9.0, 25°C
0.26
N-acetylneuraminic acid
pH 9.0, 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cf. EC 2.7.7.43
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NEUA_MOUSE
432
0
48058
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
SDS-PAGE, recombinant thioredoxin fusion protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakata, D.; Munster, A.K.; Gerardy-Schahn, R.; Aoki, N.; Matsuda, T.; Kitajima, K.
Molecular cloning of a unique CMP-sialic acid synthetase that effectively utilizes both deaminoneuraminic acid (KDN) and N-acetylneuraminic acid (Neu5Ac) as substrates
Glycobiology
11
685-692
2001
Mus musculus (Q99KK2), Oncorhynchus mykiss (Q90WG6)
Manually annotated by BRENDA team