KEGG ENZYME: 6.2.1.57

ENZYME: 6.2.1.57

Entry

EC 6.2.1.57                 Enzyme

Name

long-chain fatty acid adenylase/transferase FadD23;
fadD23 (gene name);
long-chain fatty acid adenylyltransferase FadD23

Class

Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases

Sysname

palmitate:holo-[(hydroxy)phthioceranic acid synthase] ligase

Reaction(IUBMB)

(1) ATP + stearate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + diphosphate + a stearoyl-[(hydroxy)phthioceranic acid synthase] (overall reaction);
(1a) ATP + stearate = diphosphate + (stearoyl)adenylate [RN:R12393];
(1b) (stearoyl)adenylate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + a stearoyl-[(hydroxy)phthioceranic acid synthase];
(2) ATP + palmitate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + diphosphate + a palmitoyl-[(hydroxy)phthioceranic acid synthase] (overall reaction);
(2a) ATP + palmitate = diphosphate + (palmitoyl)adenylate [RN:R12396];
(2b) (palmitoyl)adenylate + a holo-[(hydroxy)phthioceranic acid synthase] = AMP + a palmitoyl-[(hydroxy)phthioceranic acid synthase]

Reaction(KEGG)

R12393 R12396;
(other) R12394 R12395 R12397 R12398

Substrate

ATP [CPD:C00002];
stearate [CPD:C01530];
holo-[(hydroxy)phthioceranic acid synthase];
(stearoyl)adenylate [CPD:C22132];
palmitate [CPD:C00249];
(palmitoyl)adenylate [CPD:C22135]

Product

AMP [CPD:C00020];
diphosphate [CPD:C00013];
stearoyl-[(hydroxy)phthioceranic acid synthase] [CPD:C22134];
(stearoyl)adenylate [CPD:C22132];
palmitoyl-[(hydroxy)phthioceranic acid synthase] [CPD:C22124];
(palmitoyl)adenylate [CPD:C22135]

Comment

This mycobacterial enzyme activates palmitate and stearate by adenylation, followed by their loading onto the polyketide synthase EC 2.3.1.287, phthioceranic/hydroxyphthioceranic acid synthase.

History

EC 6.2.1.57 created 2019

Orthology

K12425

long-chain fatty acid adenylase/transferase FadD23

Genes

MTU:	Rv3826(fadD23)

MTV:

RVBD_3826

MTC:

MT3934

MRA:	MRA_3866(fadD23)

MTF:	TBFG_13860

MTB:	TBMG_03873

MTK:	TBSG_03896

MTZ:	TBXG_003843

MTG:	MRGA327_23565

MTE:	CCDC5079_3557

MTUR:

CFBS_4057(fadD23)

MTL:	CCDC5180_3505

MTO:	MTCTRI2_3905(fadD23)

MTD:	UDA_3826(fadD23)

MTN:	ERDMAN_4193(fadD23)

MTJ:	J112_20570

MTUB:

MT7199_3895

MTUC:

J113_26780

MTUE:

J114_20445

MTX:	M943_19645

MTUL:

TBHG_03764

MTUT:

HKBT1_4039(fadD23)

MTUU:

HKBT2_4049(fadD23)

MTQ:	HKBS1_4052(fadD23)

MBO:	BQ2027_MB3856(fadD23)

MBB:	BCG_3889(fadD23)

MBT:	JTY_3891(fadD23)

MBK:	K60_039700

MBX:

BCGT_3691

MAF:	MAF_38410(fadD23)

MMIC:

RN08_4224

MCE:	MCAN_38451(fadD23)

MCQ:	BN44_120236(fadD)

MCV:	BN43_90343(fadD)

MCX:	BN42_90354(fadD)

MCZ:	BN45_110188(fadD)

MORY:

MO_003978(fadD23)

MGAU:

MGALJ_58670(fadD23)

» show all

Reference

1 [PMID:17389997]

Authors

Gokhale RS, Saxena P, Chopra T, Mohanty D

Title

Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids.

Journal

Nat Prod Rep 24:267-77 (2007)
DOI:10.1039/b616817p

Reference

2 [PMID:17768256]

Authors

Lynett J, Stokes RW

Title

Selection of transposon mutants of Mycobacterium tuberculosis with increased macrophage infectivity identifies fadD23 to be involved in sulfolipid production and association with macrophages.

Journal

Microbiology 153:3133-40 (2007)
DOI:10.1099/mic.0.2007/007864-0

Sequence

[mtu:Rv3826]

Other DBs

ExplorEnz - The Enzyme Database:

6.2.1.57

IUBMB Enzyme Nomenclature:

6.2.1.57

ExPASy - ENZYME nomenclature database:

6.2.1.57

BRENDA, the Enzyme Database:

6.2.1.57

DBGET integrated database retrieval system