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Information on EC 4.1.2.42 - D-threonine aldolase and Organism(s) Arthrobacter sp and UniProt Accession O82872

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.42 D-threonine aldolase
IUBMB Comments
A pyridoxal-phosphate protein that is activated by divalent metal cations (e.g. Co2+, Ni2+, Mn2+ or Mg2+) [1,2]. The reaction is reversible, which can lead to the interconversion of D-threonine and D-allothreonine . Several other D-beta-hydroxy-alpha-amino acids, such as D-beta-phenylserine, D-beta-hydroxy-alpha-aminovaleric acid and D-beta-3,4-dihydroxyphenylserine, can also act as substrate .
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Arthrobacter sp
UNIPROT: O82872
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
d-threonine aldolase, axdta, low specificity d-threonine aldolase, crdta, more
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
D-threonine acetaldehyde-lyase (glycine-forming)
A pyridoxal-phosphate protein that is activated by divalent metal cations (e.g. Co2+, Ni2+, Mn2+ or Mg2+) [1,2]. The reaction is reversible, which can lead to the interconversion of D-threonine and D-allothreonine [1]. Several other D-beta-hydroxy-alpha-amino acids, such as D-beta-phenylserine, D-beta-hydroxy-alpha-aminovaleric acid and D-beta-3,4-dihydroxyphenylserine, can also act as substrate [1].
CAS REGISTRY NUMBER
COMMENTARY hide
87588-22-5
-
9024-06-0
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DTA_ARTSP
379
0
40031
Swiss-Prot
-