KEGG   ENZYME: 4.1.2.42Help
Entry
EC 4.1.2.42                 Enzyme                                 

Name
D-threonine aldolase;
D-TA;
DTA;
low specificity D-TA;
low specificity D-threonine aldolase
Class
Lyases;
Carbon-carbon lyases;
Aldehyde-lyases
BRITE hierarchy
Sysname
D-threonine acetaldehyde-lyase (glycine-forming)
Reaction(IUBMB)
(1) D-threonine = glycine + acetaldehyde [RN:R08195];
(2) D-allothreonine = glycine + acetaldehyde [RN:R08196]
Reaction(KEGG)
Substrate
D-threonine [CPD:C00820];
D-allothreonine [CPD:C12317]
Product
glycine [CPD:C00037];
acetaldehyde [CPD:C00084]
Comment
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].
History
EC 4.1.2.42 created 2007
Orthology
K19967  
D-threonine aldolase
Genes
BPE: 
BPC: 
BPER: 
BPET: 
BPEU: 
BPAR: 
BBR: 
BBM: 
BBH: 
BBX: 
BPT: 
BAV: 
BHO: 
BHM: 
BHZ: 
AXY: 
AXO: 
AXN: 
AXS: 
DAC: 
DEL: 
 » show all
Taxonomy
Reference
1  [PMID:9346293]
  Authors
Kataoka M, Ikemi M, Morikawa T, Miyoshi T, Nishi K, Wada M, Yamada H, Shimizu S.
  Title
Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38.
  Journal
Eur. J. Biochem. 248 (1997) 385-93.
  Sequence
Reference
2  [PMID:9642221]
  Authors
Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H.
  Title
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.
  Journal
J. Biol. Chem. 273 (1998) 16678-85.
  Sequence
Reference
3  [PMID:10390816]
  Authors
Liu JQ, Odani M, Dairi T, Itoh N, Shimizu S, Yamada H.
  Title
A new route to L-threo-3-[4-(methylthio)phenylserine], a key intermediate for the synthesis of antibiotics: recombinant low-specificity D-threonine aldolase-catalyzed stereospecific resolution.
  Journal
Appl. Microbiol. Biotechnol. 51 (1999) 586-91.
Reference
4  [PMID:10952004]
  Authors
Liu JQ, Odani M, Yasuoka T, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H.
  Title
Gene cloning and overproduction of low-specificity D-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for parkinsonism drug.
  Journal
Appl. Microbiol. Biotechnol. 54 (2000) 44-51.
  Sequence
Reference
5
  Authors
Liu, J.Q., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S. and Yamada, H.
  Title
Diversity of microbial threonine aldolases and their application.
  Journal
J. Mol. Catal. B 10 (2000) 107-115.
Reference
6  [PMID:12686135]
  Authors
Paiardini A, Contestabile R, D'Aguanno S, Pascarella S, Bossa F.
  Title
Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes.
  Journal
Biochim. Biophys. Acta. 1647 (2003) 214-9.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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