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IUBMB Comments A pyridoxal 5′-phosphate enzyme. This bacterial enzyme, characterized from the marine bacterium Vibrio splendidus , expands the substrate scope of a widespread pathway for the degradation of 2-aminoethylphosphonate. The enzyme is highly specific and does not act on the S enantiomer of 1-hydroxy-2-aminoethylphosphonate or other structurally related compounds.
Reaction Schemes
(1R)-(2-amino-1-hydroxyethyl)phosphonate
=
+
Synonyms pbfA ,
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pbfA
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-
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(1R)-(2-amino-1-hydroxyethyl)phosphonate = (E)-2-aminoethenylphosphonate + H2O
(1a)
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(1R)-(2-amino-1-hydroxyethyl)phosphonate = phosphonoacetaldehyde + NH3
overall reaction
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(E)-2-aminoethenylphosphonate + H2O = phosphonoacetaldehyde + NH3
(1b)
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-
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(1R)-(2-amino-1-hydroxyethyl)phosphonate ammonia-lyase
A pyridoxal 5'-phosphate enzyme. This bacterial enzyme, characterized from the marine bacterium Vibrio splendidus, expands the substrate scope of a widespread pathway for the degradation of 2-aminoethylphosphonate. The enzyme is highly specific and does not act on the S enantiomer of 1-hydroxy-2-aminoethylphosphonate or other structurally related compounds.
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(1R)-(2-amino-1-hydroxyethyl)phosphonate
phosphonoacetaldehyde + NH3
additional information
?
-
(1R)-(2-amino-1-hydroxyethyl)phosphonate
phosphonoacetaldehyde + NH3
Substrates: overall reaction, very high substrate specificity
?
(1R)-(2-amino-1-hydroxyethyl)phosphonate
phosphonoacetaldehyde + NH3
Substrates: overall reaction, very high substrate specificity
?
additional information
?
-
Substrates: the enzyme is not active toward (1S)-(2-amino-1-hydroxyethyl)phosphonate or ethanolamine and DL-isoserine
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additional information
?
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Substrates: the enzyme is not active toward (1S)-(2-amino-1-hydroxyethyl)phosphonate or ethanolamine and DL-isoserine
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(1R)-(2-amino-1-hydroxyethyl)phosphonate
phosphonoacetaldehyde + NH3
(1R)-(2-amino-1-hydroxyethyl)phosphonate
phosphonoacetaldehyde + NH3
Substrates: overall reaction, very high substrate specificity
?
(1R)-(2-amino-1-hydroxyethyl)phosphonate
phosphonoacetaldehyde + NH3
Substrates: overall reaction, very high substrate specificity
?
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pyridoxal 5'-phosphate
dependent on
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Mg2+
5 mM used in assay conditions
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0.43
(1R)-(2-amino-1-hydroxyethyl)phosphonate
at pH 8.0 and 25°C
-
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5.3
(1R)-(2-amino-1-hydroxyethyl)phosphonate
at pH 8.0 and 25°C
-
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12.3
(1R)-(2-amino-1-hydroxyethyl)phosphonate
at pH 8.0 and 25°C
-
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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PBFA_VIBS1
Vibrio splendidus (strain 12B01)
479
0
52703
Swiss-Prot
Chloroplast (Reliability: 5 )
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His-Select cobalt affinity column chromatography, and Superdex 200 gel filtration
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expressed in Escherichia coli BL21 Star cells
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Zangelmi, E.; Stankovic, T.; Malatesta, M.; Acquotti, D.; Pallitsch, K.; Peracchi, A.
Discovery of a new, recurrent enzyme in bacterial phosphonate degradation (R)-1-hydroxy-2-aminoethylphosphonate ammonia-lyase
Biochemistry
60
1214-1225
2021
Vibrio splendidus (A3UZK3), Vibrio splendidus 12B01 (A3UZK3)
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