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

BRENDA support

Literature summary extracted from

  • Murray, B.W.; Takayama, S.; Schultz, J.; Wong, C.H.
    Mechanism and specificity of human alpha-1,3-fucosyltransferase V (1996), Biochemistry, 35, 11183-11195.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.152 deoxyfuconojirimycin modest inhibitor, causes 21% inhibition, synergism: combined with GDP at their Ki levels results in 80% inhibition, combined with GMP causes 50.4% inhibition Homo sapiens
2.4.1.152 GDP causes 22% inhibition Homo sapiens
2.4.1.152 GDP-alpha-D-glucose
-
Homo sapiens
2.4.1.152 GDP-alpha-D-mannose
-
Homo sapiens
2.4.1.152 GDP-fucose
-
Homo sapiens
2.4.1.152 GMP causes 23% inhibition Homo sapiens
2.4.1.152 GTP potent inhibitor Homo sapiens
2.4.1.152 Inosine diphosphate potent inhibitor Homo sapiens
2.4.1.152 L-fucal modest inhibitor, causes 26% inhibition, combined with GDP causes 40% inhibition Homo sapiens
2.4.1.152 additional information
-
Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.152 0.025
-
GDP-fucose LacNAcbeta-O-(CH2)5CO2CH3 as substrate Homo sapiens
2.4.1.152 0.06
-
GDP-fucose LacNAc as substrate Homo sapiens
2.4.1.152 0.17
-
LacNAcbeta-O-(CH2)5CO2CH3
-
Homo sapiens
2.4.1.152 1.2
-
Co2+
-
Homo sapiens
2.4.1.152 6.1
-
Mn2+
-
Homo sapiens
2.4.1.152 6.7
-
Ca2+
-
Homo sapiens
2.4.1.152 8.6
-
Mg2+
-
Homo sapiens
2.4.1.152 8.8
-
LacNAc
-
Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.152 Ca2+ alternative divalent metal cofactor Homo sapiens
2.4.1.152 Co2+ alternative divalent metal cofactor Homo sapiens
2.4.1.152 Mg2+ alternative divalent metal cofactor Homo sapiens
2.4.1.152 Mn2+ acts as electrophilic catalyst in the nonenzymatic hydrolysis of GDP-fucose Homo sapiens
2.4.1.152 Zn2+ no activity Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.152 Homo sapiens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.152 GDP-fucose + LacNAc
-
Homo sapiens GDP + ?
-
?
2.4.1.152 GDP-fucose + LacNAcbeta-O-(CH2)5CO2CH3
-
Homo sapiens GDP + ?
-
?
2.4.1.152 additional information catalyzes the transfer of the L-fucose moiety from guanosine diphosphate-beta-L-fucose to acceptor sugars to form biologically important fucoglycoconjugates, including sialyl Lewis x, the enzyme processes acceptor sugars with either oxygen or sulfur in the GlcNAc ring, but a similar sugar structure with nitrogen in the GlcNAc ring, is an inhibitor Homo sapiens ?
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.152 5 7 in both phosphate and cacodylate buffers Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.4.1.152 0.0062
-
GDP-fucose LacNAc as substrate Homo sapiens
2.4.1.152 0.029
-
GDP
-
Homo sapiens
2.4.1.152 0.031
-
GDP-fucose LacNAcbeta-O-(CH2)5CO2CH3 as substrate Homo sapiens
2.4.1.152 0.069
-
Inosine diphosphate
-
Homo sapiens
2.4.1.152 0.29
-
GDP-alpha-D-mannose
-
Homo sapiens
2.4.1.152 0.38
-
GDP-alpha-D-glucose
-
Homo sapiens
2.4.1.152 0.7
-
GMP
-
Homo sapiens
2.4.1.152 45
-
deoxyfuconojirimycin
-
Homo sapiens
2.4.1.152 71
-
L-fucal
-
Homo sapiens