KEGG ENZYME: 4.1.2.55

KEGG

ENZYME: 4.1.2.55

Entry

EC 4.1.2.55                 Enzyme

Name

2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase;
2-keto-3-deoxygluconate aldolase (ambiguous);
KDGA (ambiguous)

Class

Lyases;
Carbon-carbon lyases;
Aldehyde-lyases

Sysname

2-dehydro-3-deoxy-6-phospho-D-gluconate/2-dehydro-3-deoxy-6-phospho-D-galactonate D-glyceraldehyde-3-phosphate-lyase (pyruvate-forming)

Reaction(IUBMB)

(1) 2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate [RN:R05605];
(2) 2-dehydro-3-deoxy-6-phospho-D-galactonate = pyruvate + D-glyceraldehyde 3-phosphate [RN:R01064]

Reaction(KEGG)

R01064 R05605;
(other) R08570 R10616

Substrate

2-dehydro-3-deoxy-6-phospho-D-gluconate [CPD:C04442];
2-dehydro-3-deoxy-6-phospho-D-galactonate [CPD:C01286]

Product

pyruvate [CPD:C00022];
D-glyceraldehyde 3-phosphate [CPD:C00118]

Comment

In the archaeon Sulfolobus solfataricus the enzyme is involved in glucose and galactose catabolism via the branched variant of the Entner-Doudoroff pathway. It utilizes 2-dehydro-3-deoxy-6-phosphate-D-gluconate and 2-dehydro-3-deoxy-6-phosphate-D-galactonate with similar catalytic efficiency. In vitro the enzyme can also catalyse the cleavage of the non-phosphorylated forms 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate with much lower catalytic efficiency. cf. EC 4.1.2.21, 2-dehydro-3-deoxy-6-phosphogalactonate aldolase, and EC 4.1.2.14, 2-dehydro-3-deoxy-phosphogluconate aldolase.

History

EC 4.1.2.55 created 2014

Pathway

Pentose phosphate pathway

Galactose metabolism

Metabolic pathways

Microbial metabolism in diverse environments

Orthology

2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase

Genes

TAC:

Ta0619

TVO:	TVG0663048(TVG0663048)

PTO:

PTO1026

FAC:	FACI_IFERC01G1727

FAI:

FAD_0700

STO:	STK_24790(kdgA)

SOH:	D1869_13570

SSO:	SSO3197(eda)

SOL:

Ssol_0934

SULA_0967

SULB_0969

SULC_0968

J5U23_00301

SACC_31320

SAI:

Saci_0225

SacN8_01090

SacRon12I_01090

SUSAZ_01130

SIS:	LS215_2326

SIA:	M1425_2163

SIM:	M1627_2243

SID:

M164_2166

SIY:	YG5714_2289

SIN:	YN1551_0626

SII:

LD85_2429

SIH:

SiH_2108

SIR:

SiRe_2040

SIC:

SiL_2015

BFU36_06090

GFS03_11780

GFS33_03590

EWF20_14570

MSE:

Msed_1296

MJ1HA_1503

MCN:

Mcup_0949

MHK:	DFR87_12295

DFR88_11840

GWK48_00445

MJN:	MjAS7_2363

AHO:

Ahos_0260

B6F84_04920

DFR85_02045 DFR85_14740

DFR86_04380

D1866_07690

HS5_15430

HS1genome_1556

D1868_10845

KN1_14740

IC006_2133

RQ359_002107

HS7_04580

PAS:

Pars_1388

PYR:

P186_1933

POG:

Pogu_0825

TTN:	TTX_1156a(kdgA)

TUZ:

TUZN_0957

Reference

1 [PMID:10527934]

Authors

Buchanan CL, Connaris H, Danson MJ, Reeve CD, Hough DW

Title

An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates.

Journal

Biochem J 343 Pt 3:563-70 (1999)
DOI:10.1042/bj3430563

Sequence

Reference

2 [PMID:16330030]

Authors

Lamble HJ, Theodossis A, Milburn CC, Taylor GL, Bull SD, Hough DW, Danson MJ

Title

Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the archaeon Sulfolobus solfataricus.

Journal

FEBS Lett 579:6865-9 (2005)
DOI:10.1016/j.febslet.2005.11.028

Sequence

Reference

3 [PMID:17176250]

Authors

Wolterink-van Loo S, van Eerde A, Siemerink MA, Akerboom J, Dijkstra BW, van der Oost J

Title

Biochemical and structural exploration of the catalytic capacity of Sulfolobus KDG aldolases.

Journal

Biochem J 403:421-30 (2007)
DOI:10.1042/BJ20061419

Sequence

[sso:SSO3197] [sai:Saci_0225] [sto:STK_24790]

Other DBs

ExplorEnz - The Enzyme Database:

IUBMB Enzyme Nomenclature:

ExPASy - ENZYME nomenclature database:

BRENDA, the Enzyme Database:

DBGET integrated database retrieval system