Information on EC 1.14.18.2 - CMP-N-acetylneuraminate monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.18.2
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RECOMMENDED NAME
GeneOntology No.
CMP-N-acetylneuraminate monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+ = CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
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-
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reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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CMP-N-glycoloylneuraminate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
CMP-N-acetylneuraminate,ferrocytochrome-b5:oxygen oxidoreductase (N-acetyl-hydroxylating)
This enzyme contains both a Rieske-type [2Fe-2S] cluster and a second iron site. The ferricytochrome b5 produced is reduced by NADH and cytochrome-b5 reductase (EC 1.6.2.2). The enzyme can be activated by Fe2+ or Fe3+.
CAS REGISTRY NUMBER
COMMENTARY hide
116036-67-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Muelleria sp.
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-
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Manually annotated by BRENDA team
no activity in Gallus gallus
BLAST analysis of the genome does not reveal the existence of a similar protein structure
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Manually annotated by BRENDA team
no activity in Homo sapiens
no activity in Ornithorhynchus anatinus
BLAST analysis of the genome does not reveal the existence of a similar protein structure
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-
Manually annotated by BRENDA team
no activity in Taeniopygia guttata
BLAST analysis of the genome does not reveal the existence of a similar protein structure
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CMP-N-acetylneuraminate + 6,7-dimethyl-5,6,7,8-tetrahydrobiopterin + O2
CMP-N-glycoloylneuraminate + ?
show the reaction diagram
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less effectiove than NADH or NADPH
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?
CMP-N-acetylneuraminate + ascorbic acid + O2
CMP-N-glycoloylneuraminate + dehydroascorbate + H2O
show the reaction diagram
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2
CMP-N-glycoloylneuraminate + ferricytrochrome b5 + H2O
show the reaction diagram
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2 + H+
CMP-N-glycoloylneuraminate + ferricytochrome b5 + H2O
show the reaction diagram
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
show the reaction diagram
CMP-N-acetylneuraminate + NADPH + O2
CMP-N-glycoloylneuraminate + NADP+ + H2O
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2 + H+
CMP-N-glycoloylneuraminate + ferricytochrome b5 + H2O
show the reaction diagram
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ferrocytochrome b5
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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in cofactor ferrocytochrome b5
FeSO4
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activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2,2'-dipyridyl
3'-AMP
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5 mM, complete inhibition
3'-CMP
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5 mM, about 20% inhibition
3'-UMP
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5 mM, about 90% inhibition
5'-AMP
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5 mM, about 78% inhibition
5'-UMP
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5 mM, about 15% inhibition
anti-(rat cytochrome b5) antiserum
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Ca2+
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0.5 mM, 12% inhibition
cardiolipin
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3 mM, 15% inhibition
CHAPS
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15 mM, complete inhibition
cholic acid
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10 mM, 89% inhibition
CMP-N-glycoloylneuraminate
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Co2+
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Cu2+
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decylglucopyranoside
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5 mM, 22% inhibition
ferrozine
Hg2+
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slight inhibition
Mg2+
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Na2HPO4
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2 mM, 86% inhibition
Na4P2O7
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2 mM, 54% loss of activity
NaCl
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above 100 mM
Ni2+
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octylglucopyranoside
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30 mM, 48% inhibition
phosphatidic acid
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3 mM, 20% inhibition
phosphatidylinositol
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3 mM, 68% inhibition
Tiron
Zn2+
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Zwittergent 3-12
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5 mM, 40% inhibition
additional information
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not inhibited by increased ionic strength, no inhibition by 1 M NaCl
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
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activates
decyl glucoside
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activation
dithiothreitol
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activates
glutathione
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activates
Nonidet P-40
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effective inhibitor
Octanoic acid
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1 mM, modest activation
octyl glucoside
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effective inhibitor
SDS
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1 mM, modest activation
Triton X-100
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effective inhibitor
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 2.5
CMP-N-acetylneuraminate
0.0029 - 0.0032
ferrocytochrome b5
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00093
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0.126
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0.816
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.4
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6 - 6.6
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6.4 - 7.4
6.8 - 7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 6.8
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about 60% of maximal activity at pH 5.6 and pH 6.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 27
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25 - 33
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 43
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15C: about 55% of maximal activity, 43C: about 30% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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generation of a stable CHO cell line with significantly reduced levels of CMP-Neu5Ac hydroxylase activity and reduced amounts of N-glycolylneuraminic acid, using a rational antisense RNA strategy
Manually annotated by BRENDA team
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weak activity
Manually annotated by BRENDA team
C1K3L2
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Manually annotated by BRENDA team
C1K3L2
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Manually annotated by BRENDA team
C1K3L2
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Manually annotated by BRENDA team
cDNA generated from, mRNA highly expressed
Manually annotated by BRENDA team
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weak activity
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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from thymus, spleen, lymph node and peripheral blood. Highest activity in peripheral blood lymphocytes
Manually annotated by BRENDA team
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traces of Neu5Gc found in serum by paper chromatography and in serum glycoproteins by HPLC analysis of per-O-benzoylated sialic acids
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
C1K3L2
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Manually annotated by BRENDA team
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naturally occuring truncated protein lacking 46 amino acids in the middle of the normal full-length protein
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17000
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gel filtration
56000
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gel filtration
58000
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gel filtration
60000
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gel filtration
64000
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1 * 64000, SDS-PAGE
65000
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1 * 65000, SDS-PAGE
75000
C1K3L2
determined by SDS-PAGE and Western Blot analysis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
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a main protein of 76000 da and a minor protein of 64000 Da correlates with CMP-neu5Ac hydroxylase activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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48 h, 10% loss of activity
25
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2 h, 50% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10 mM in the initial homogenization buffer is required for stability during 60-90 min incubation
after each cycle of freezing and thawing, 25% loss of activity
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enzyme is greatly stabilized by CMP-N-acetylneuraminate
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, stable in crude extract for several weeks
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-80 C, 0.2 mM CMP-N-acetylneuraminate, stable for at least 6 months
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-80 C, very stable
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4C, 48 h, 10% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cell extracts are prepared
C1K3L2
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination of wild-type and mutant alleles, genotyping and expression analysis, overview
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expressed in pig kidney PK15 cells and human vascular endothelial ECV304 cells
expression in Cos-1 cells
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expression in Escherichia coli
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full-length CMAH cDNA is cloned from umbilical cord blood mononuclear cells and HeLa cells into the pGEM-T easy vector for sequencing, GFP- or FLAG-tagged constructs are prepared using the vectors pFLAG-CMV-2 and pEGFP-C2/pEGFP-C1
C1K3L2
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G1266A
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naturally occuring silent mtation
G139A
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naturally occuring missense mutation
G1600A
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naturally occuring silent mtation
T265A
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naturally occuring missense mutation
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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enzyme is used for the detection of human cancer like colon cancer, melanoma, retinoblastoma cell lines and tissues, germ cell tumours and breast cancer by detection of N-glycolylneuraminic acid-containing glycolipids
medicine
C1K3L2
the results pinpoint the crucial need for totally xenofree culturing and expansion conditions for human therapeutic stem cells