KEGG   ENZYME: 4.1.2.42
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
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)
R08195 R08196
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
VCY: IX92_24510
VCT: JV59_23355
MVS: MVIS_1700
MMAA: FR932_08675
LPC: LPC_1948
LPA: lpa_03685
LFA: LFA_1474 LFA_1475
LSH: CAB17_00325
TMC: LMI_2673
NBA: CUN60_03800
RME: Rmet_4194
CGD: CR3_3495
PPNO: DA70_23570
PPNM: LV28_07140
PPUL: RO07_01255
PSPU: NA29_10435
PAPI: SG18_01440
BPE: BP0453
BPC: BPTD_0480
BPER: BN118_0425
BPET: B1917_3586
BPEU: Q425_38740
BPAR: BN117_4500
BBR: BB4953
BPT: Bpet0041
BAV: BAV3375
BHO: D560_1496
BHM: D558_1488
POL: Bpro_4819
AJS: Ajs_0490
DAC: Daci_4362
RTA: Rta_07170
HYB: Q5W_00455
MPT: Mpe_A0329
HAR: HEAR2724
OCA: OCAR_6698
MSL: Msil_3403
RBM: TEF_08225
PZU: PHZ_c1004
SPHI: TS85_22560
PSEA: WY02_26120
PSEE: FRP1_16835
PSEH: XF36_16330
PAUT: Pdca_45830
STI: Sthe_1797
PSL: Psta_1894
PLM: Plim_2914
IPA: Isop_2867
SACI: Sinac_5761
CPI: Cpin_7000
MUC: MuYL_2134
DFE: Dfer_1026
SLI: Slin_1233
FAE: FAES_4155
MARM: YQ22_06060
 » show all
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 248:385-93 (1997)
DOI:10.1111/j.1432-1033.1997.00385.x
  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 273:16678-85 (1998)
DOI:10.1074/jbc.273.27.16678
  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 51:586-91 (1999)
DOI:10.1007/s002530051436
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 54:44-51 (2000)
DOI:10.1007/s002539900301
  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 10:107-115 (2000)
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 1647:214-9 (2003)
DOI:10.1016/S1570-9639(03)00050-5
Other DBs
ExplorEnz - The Enzyme Database: 4.1.2.42
IUBMB Enzyme Nomenclature: 4.1.2.42
ExPASy - ENZYME nomenclature database: 4.1.2.42
BRENDA, the Enzyme Database: 4.1.2.42
LinkDB

DBGET integrated database retrieval system