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Literature summary for 4.1.1.81 extracted from

  • Tavares, N.K.; Zayas, C.L.; Escalante-Semerena, J.C.
    The Methanosarcina mazei MM2060 gene encodes a bifunctional kinase/decarboxylase enzyme involved in cobamide biosynthesis (2018), Biochemistry, 57, 4478-4495 .
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Methanosarcina mazei Q8PVB1 bifunctional enzyme with L-threonine-O-3-phosphate decarboxylase (EC 4.1.1.81) and L-Thr kinase activities (EC 2.7.1.177)
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Methanosarcina mazei Goe1 Q8PVB1 bifunctional enzyme with L-threonine-O-3-phosphate decarboxylase (EC 4.1.1.81) and L-Thr kinase activities (EC 2.7.1.177)
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Purification (Commentary)

Purification (Comment) Organism
when purified under anoxic conditions, CobD displayed Michaelis-Menten kinetics and has 1000fold higher affinity for ATP and 1300fold higher catalytic efficiency than CobD purified under oxic conditions Methanosarcina mazei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-threonine O-3-phosphate
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Methanosarcina mazei (R)-1-aminopropan-2-yl phosphate + CO2
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?
L-threonine O-3-phosphate
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Methanosarcina mazei Goe1 (R)-1-aminopropan-2-yl phosphate + CO2
-
?
additional information bifunctional enzyme with L-threonine-O-3-phosphate decarboxylase (EC 4.1.1.81) and L-Thr kinase activities (EC 2.7.1.177). Using ATP and L-Thr as substrates, the enzyme generates ADP, L-Thr-P, and (R)-1-aminopropan-2-ol O-phosphate as products. No substrate: L-serine phosphate Methanosarcina mazei ?
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?
additional information bifunctional enzyme with L-threonine-O-3-phosphate decarboxylase (EC 4.1.1.81) and L-Thr kinase activities (EC 2.7.1.177). Using ATP and L-Thr as substrates, the enzyme generates ADP, L-Thr-P, and (R)-1-aminopropan-2-ol O-phosphate as products. No substrate: L-serine phosphate Methanosarcina mazei Goe1 ?
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?

Synonyms

Synonyms Comment Organism
CobD
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Methanosarcina mazei
MM2060
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Methanosarcina mazei

General Information

General Information Comment Organism
physiological function CobD is able to complement a Salmonella enterica CobD mutant Methanosarcina mazei