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Sequence of DTA_ARTSP

EC Number:4.1.2.42

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
D-threonine aldolase
O82872
Arthrobacter sp
379
40031
Reaction
D-allothreonine = glycine + acetaldehyde
Other sequences found for EC No. 4.1.2.42

General information:

Sequence
  0 MSQEVIRGIA LPPPAQPGDP LARVDTPSLV LDLAPFEANL RAMQAWADRH DVALRPHAKA
 60 HKCPEIALRQ LALGARGICC QKVSEALPFV AAGIQDIHIS NEVVGPAKLA LLGQLARVAK
120 ISVCVDNAHN LSQVSQAMVQ AGAQIDVLVE VDVGQGRCGV SDDALVLALA QQARDLPGVN
180 FAGLQAYHGS VQHYRTREER AEVCRQAARI AASYAQLLRE SGIACDTITG GGTGSAEFDA
240 ASGVYTELQA GSYAFMDGDY GANEWDGPLA FENSLFVLAT VMSKPAPDRV ILDAGLKSTT
300 AECGPPAIFG EPGLTYTAIN DEHGVVRVEP GAQAPDLGAV LRLVPSHVDP TFNLHDGLVV
360 VRDGVVEDIW EISARGFSR
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
792194
Liu J.-Q.,Dairi T.,Itoh N.,Kataoka M.,Shimizu S.,Yamada H.
A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. Strain DK-38. Molecular cloning and cofactor characterization.
J. Biol. Chem.
273
16678-16685
1998
792195
Kataoka M.,Ikemi M.,Morikawa T.,Miyoshi T.,Nishi K.,Wada M.,Yamada H.,Shimizu S.
Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38.
Eur. J. Biochem.
248
385-393
1997