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Literature summary for 2.7.1.82 extracted from

  • Faulkner, A.; Turner, J.M.
    Phosphorylation of ethanolamine in catabolism. Biodegradative adenosine triphosphate-ethanolamine phosphotransferase and related enzymes in bacteria (1974), Biochem. Soc. Trans., 2, 133-136.
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.36
-
DL-1-aminopropan-2-ol
-
Flavobacterium rhenanum
0.5
-
ATP
-
Achromobacter sp.
0.5
-
ATP
-
Microbacterium arborescens
0.5
-
ATP
-
Flavobacterium rhenanum
0.53
-
ethanolamine
-
Flavobacterium rhenanum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ Mg2+ required Achromobacter sp.
Mg2+ Mg2+ required Microbacterium arborescens
Mg2+ Mg2+ required Flavobacterium rhenanum
Mg2+ maximum concentration equal to that of ATP Achromobacter sp.
Mg2+ maximum concentration equal to that of ATP Microbacterium arborescens
Mg2+ maximum concentration equal to that of ATP Flavobacterium rhenanum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + ethanolamine Achromobacter sp.
-
ADP + O-phosphoethanolamine
-
?
ATP + ethanolamine Microbacterium arborescens
-
ADP + O-phosphoethanolamine
-
?
ATP + ethanolamine Flavobacterium rhenanum
-
ADP + O-phosphoethanolamine
-
?
additional information Achromobacter sp. bacteria: enzyme functions in a biodegradative mode, higher organisms: biosynthetic function ?
-
?
additional information Microbacterium arborescens bacteria: enzyme functions in a biodegradative mode, higher organisms: biosynthetic function ?
-
?
additional information Flavobacterium rhenanum bacteria: enzyme functions in a biodegradative mode, higher organisms: biosynthetic function ?
-
?

Organism

Organism UniProt Comment Textmining
Achromobacter sp.
-
NCIB 9205
-
Flavobacterium rhenanum
-
NCIB 9157, enzyme formed only when amino alcohol serves as a substrate and when activated by ADP
-
Microbacterium arborescens
-
NCIB 8185, enzyme formed only when amino alcohol serves as a substrate and when activated by ADP
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + DL-1-aminopropan-2-ol
-
Achromobacter sp. ADP + DL-1-aminopropane 2-phosphate
-
?
ATP + DL-1-aminopropan-2-ol
-
Microbacterium arborescens ADP + DL-1-aminopropane 2-phosphate
-
?
ATP + DL-1-aminopropan-2-ol
-
Flavobacterium rhenanum ADP + DL-1-aminopropane 2-phosphate
-
?
ATP + ethanolamine
-
Achromobacter sp. ADP + O-phosphoethanolamine
-
?
ATP + ethanolamine
-
Microbacterium arborescens ADP + O-phosphoethanolamine
-
?
ATP + ethanolamine
-
Flavobacterium rhenanum ADP + O-phosphoethanolamine
-
?
additional information bacteria: enzyme functions in a biodegradative mode, higher organisms: biosynthetic function Achromobacter sp. ?
-
?
additional information bacteria: enzyme functions in a biodegradative mode, higher organisms: biosynthetic function Microbacterium arborescens ?
-
?
additional information bacteria: enzyme functions in a biodegradative mode, higher organisms: biosynthetic function Flavobacterium rhenanum ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Flavobacterium rhenanum

Cofactor

Cofactor Comment Organism Structure
ADP stimulates Flavobacterium rhenanum