KEGG ENZYME: 4.1.2.42

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

Pathway

ec00470

D-Amino acid metabolism

ec01100

Metabolic pathways

Orthology

K19967

D-threonine aldolase

Genes

RPJ:	N234_30730 N234_35660

CUH:	BJN34_31445

RME:

Rmet_4194

CTI:	RALTA_B0772

CBW:	RR42_s1597

CGD:

CR3_3495

CCUP:

BKK81_29480

CUP:	BKK80_26875

CUU:	BKK79_32780

CPAU:

EHF44_19035

COX:	E0W60_02755

BYI:	BYI23_D007720

BUE:	BRPE67_DCDS09630

PPK:	U875_06500

PPNO:

DA70_23570

PPNM:

LV28_07140

PRB:	X636_03075

PPUL:

RO07_01255

PSPU:

NA29_10435

PAPI:

SG18_01440

PVE:	UC34_17480

POX:	MB84_22255

PTX:	ABW99_15240

PFG:	AB870_04515

PNR:	AT302_14610

PAND:

DRB87_16120

PFIB:

PI93_010510

BUO:	BRPE64_DCDS04080

BPE:

BP0453

BPC:

BPTD_0480

BPER:

BN118_0425

BPET:

B1917_3586

BPEU:

Q425_38740

BPAR:

BN117_4500

BBH:	BN112_3472

BBR:

BB4953

BBM:	BN115_4610

BBX:	BBS798_4731

BPT:

Bpet0041

BAV:

BAV3375

BHO:

D560_1496

BHM:

D558_1488

BHZ:	ACR54_04567

BTRM:

SAMEA390648701156

BBRO:

BAU06_00460

BFZ:	BAU07_00325

BPDZ:

BBN53_00315

BOH:	AKI39_00870

BGM:	CAL15_00545

AXY:	AXYL_00071

AXO:	NH44784_021281

AXN:	AX27061_0078

AXX:	ERS451415_00076

ADT:	APT56_00670

AIS:	BUW96_26095

ASW:	CVS48_05695

ACHR:

C2U31_05340

ACHB:

DVB37_00340

ADY:	HLG70_21350

PUS:	CKA81_14160

ODI:

ODI_R0236

BOZ:	DBV39_05120

PACR:

FXN63_08015

PARK:

LSG25_15325

RHY:	RD110_05405

POL:	Bpro_4092 Bpro_4819

PNA:

Pnap_0513

AAV:

Aave_4234

AJS:

Ajs_0490

AAA:

Acav_4116

ACK:	C380_21305

ACRA:

BSY15_1982

ACID:

CBP33_02375

ACIP:

CBP36_02780

ACIN:

CBP34_02340

ACIS:

CBP35_16160

ACIO:

EAG14_19080

AMON:

H9L24_17945

VEI:

Veis_3378

DAC:

Daci_4362

DEL:	DelCs14_2466

DTS:	BI380_07650

DHK:	BO996_19575

DLA:	I6G47_02470

VPD:	VAPA_2c02520

CTT:	CtCNB1_4277

CTES:

O987_25450

CSER:

CCO03_16130

ADN:	Alide_0588

ADK:	Alide2_0553

RTA:

Rta_07170

OTO:	ADJ79_06845

OTK:	C6570_00075

HYR:	BSY239_3490

HYB:

Q5W_00455

HYL:	LPB072_19995

HYC:	E5678_13770

HYN:	F9K07_04500

HTN:	KI616_23055

DPY:	BA022_12410

DIH:	G7047_19805

DRG:	H9K76_02520

DIA:	Dtpsy_0501

MPT:

Mpe_A0329

METP:

C1M51_10865

HAR:

HEAR2724

MMS:	mma_0025 mma_0441

XYK:	GT347_11700

PAUU:

E8A73_019985

KAI:

K32_06960

BRS:

S23_11060

BSYM:

CIT39_26400

BBET:

F8237_20440

RBK:	E0H22_18965

OCA:

OCAR_6698

OCG:	OCA5_c13700

OCO:	OCA4_c13700

TRB:	HB776_00695

BOP:	AXW83_16940

BOS:

BSY19_202

BVV:	BHK69_03930

BOI:	BLM15_26070

BOF:	FQV39_20585

MSL:

Msil_3403

FIL:	BN1229_v1_3686

FIY:	BN1229_v1_3680

TSO:

IZ6_03930

RBM:

TEF_08225

KVL:

KVU_0190

KVU:

EIO_0640

SPHI:

TS85_22560

SPLM:

BXU08_14985

SPHC:

CVN68_15690

RGI:	RGI145_05520

ROS:	CTJ15_11875

RMUC:

FOB66_07340

SHUM:

STHU_29840

SVC:	STVA_21010

HADH:

FRZ61_50040

GYU:	FE374_14720

STI:

Sthe_1797

LCRE:

Pla8534_12090

LPAV:

PLANPX_1609

DFE:

Dfer_1026

DSN:	HWI92_05860

SINH:

LS482_21080

» 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

[ag:BAA31547]

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

[ag:BAA31547]

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

[axy:AXYL_00071]

Reference

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