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Literature summary for 5.1.3.2 extracted from

  • Gabrial, O.; Kalckar, H.M.; Darrow, R.A.
    UDP-galactose-4-epimerase (1975), ubunit enzymes: biochemistry and function (Ebner, K. B., ed.), 2, 85-135.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
5'-UMP
-
Bos taurus
5'-UMP the native enzyme is completely insensitive to inhibition, the desensitized enzyme is strongly inhibited. Desensitization by heat converts the enzyme to its ultimate catalytic form Escherichia coli
5'-UMP
-
Saccharomyces fragilis
5'-UMP
-
Torulopsis candida
5-(adenosine-5'-diphosphoryl)-D-ribose reductive inhibition Escherichia coli
5-(thymidine-5'-diphosphoryl)-D-glucose reductive inhibition Escherichia coli
5-(Thymidine-5'-diphosphoryl)-D-ribose reductive inhibition Escherichia coli
D-galactose
-
Torulopsis candida
glucose plus UMP
-
Escherichia coli
glucose plus UMP
-
Torulopsis candida
NaBH4 reductive inhibition Escherichia coli
NADH
-
Bos taurus
NADH
-
Escherichia coli
Thymidine diphospho-6-deoxy-D-xylo-4-hexosulose reductive inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.16
-
UDPgalactose
-
Escherichia coli
1.2
-
UDPgalactose
-
Torulopsis candida

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
2 * 40000, SDS-PAGE Escherichia coli
60000
-
2 * 60000, enzyme exists in an active dimeric and an active tetrameric form Kluyveromyces marxianus
60000
-
4 * 60000, enzyme exists in an active dimeric and an active tetrameric form Kluyveromyces marxianus
80000
-
sedimentation equilibrium studies Escherichia coli
120000
-
sedimentation equilibrium measurement, addition of NAD+, active dimeric enzyme form Kluyveromyces marxianus
240000
-
sedimentation equilibrium measurement, addition of NAD+, 0.01 M Tris buffer with cations, active tetrameric form Kluyveromyces marxianus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Escherichia coli
-
-
-
Kluyveromyces marxianus
-
-
-
Saccharomyces fragilis
-
-
-
Torulopsis candida
-
-
-
Vigna radiata var. radiata
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP-D-glucose
-
Escherichia coli ?
-
?
CDP-D-glucose
-
Escherichia coli ?
-
?
Deoxy-UDP-D-glucose
-
Escherichia coli ?
-
?
TDP-6-deoxy-D-galactose
-
Escherichia coli ?
-
?
TDP-D-glucose
-
Escherichia coli TDP-D-galactose
-
?
UDP-6-deoxy-D-glucose
-
Escherichia coli ?
-
?
UDP-D-fucose
-
Escherichia coli ?
-
?
UDP-D-galactose-hexodialose
-
Escherichia coli ?
-
?
UDP-D-xylose
-
Escherichia coli ?
-
?
UDP-galactose
-
Vigna radiata var. radiata UDP-glucose
-
?
UDP-galactose
-
Escherichia coli UDP-glucose
-
?
UDP-galactose
-
Bos taurus UDP-glucose
-
?
UDP-galactose
-
Saccharomyces fragilis UDP-glucose
-
?
UDP-galactose
-
Kluyveromyces marxianus UDP-glucose
-
?
UDP-galactose
-
Torulopsis candida UDP-glucose
-
?
UDP-L-arabinose
-
Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 40000, SDS-PAGE Escherichia coli
dimer 2 * 60000, enzyme exists in an active dimeric and an active tetrameric form Kluyveromyces marxianus
tetramer
-
Escherichia coli
tetramer 4 * 60000, enzyme exists in an active dimeric and an active tetrameric form Kluyveromyces marxianus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Escherichia coli
NAD+
-
Bos taurus
NAD+ depends on addition of NAD+ for catalytic acitivity, Km: 0.14 mM. Cannot be replaced by NADP+ Torulopsis candida