KEGG ENZYME: 6.3.2.35

ENZYME: 6.3.2.35

Entry

EC 6.3.2.35                 Enzyme

Name

D-alanine---D-serine ligase;
VanC;
VanE;
VanG

Class

Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)

Sysname

D-alanine:D-serine ligase (ADP-forming)

Reaction(IUBMB)

D-alanine + D-serine + ATP = D-alanyl-D-serine + ADP + phosphate [RN:R09595]

Reaction(KEGG)

R09595

Substrate

D-alanine [CPD:C00133];
D-serine [CPD:C00740];
ATP [CPD:C00002]

Product

D-alanyl-D-serine [CPD:C19719];
ADP [CPD:C00008];
phosphate [CPD:C00009]

Comment

The product of this enzyme, D-alanyl-D-serine, can be incorporated into the peptidoglycan pentapeptide instead of the usual D-alanyl-D-alanine dipeptide, which is formed by EC 6.3.2.4, D-alanine---D-alanine ligase. The resulting peptidoglycan does not bind the glycopeptide antibiotics vancomycin and teicoplanin, conferring resistance on the bacteria.

History

EC 6.3.2.35 created 2010

Orthology

K18856

D-alanine---D-serine ligase

Genes

CGOT:

J1899_06180(vanG)

ALKL:

MM271_03695(vanG)

BBE:	BBR47_05870

BFM:	BP422_28590(vanB)

BBOR:

RFB14_20030(vanG)

BRUM:

NDK47_11545(vanG) NDK47_20795(vanG)

PBJ:	VN24_01315(vanB)

PSOP:

KP014_14540(vanG)

PTHI:

NDS46_12310(vanG)

PMAH:

PTQ21_20225(vanG)

PDY:	QJQ58_09795(vanG)

PSPN:

L1F29_01965(vanG)

PPAB:

KET34_16100(vanG)

PEZZ:

HW560_23690(vanG)

CHEB:

HH215_23270(vanG)

PLIG:

NAG76_22720

SANS:

DK43_03860(vanB)

ECAS:

ECBG_02849

EGA:	AL523_09465

EIE:	ENLAB_26750(ddlA_2)

ENI:	CXM95_04560

VCP:	H9L18_13855(vanC)

VFV:	K5K99_04105(vanC)

CLB:	Clo1100_2030

CACE:

CACET_c25480(vanA)

CFM:	BJL90_20410(vanB)

CARG:

RSJ17_11295(vanB)

CIU:	G4D55_13020

RPAY:

P0092_11950(vanG)

FPLA:

A4U99_10115(vanB)

RGV:	NQ502_15010(vanG)

OVA:

OBV_09510

PFAA:

MM59RIKEN_12790(vanG)

VCOP:

MM50RIKEN_08120(vanG)

LASA:

L9O85_05970

OKO:	Ruko_33060(vanG)

CFEM:

HCR03_19250(vanG)

DGI:	Desgi_1749

IBU:	IB211_01760

CSO:

CLS_04660

LXA:	OW255_13715(vanG)

HSD:	SD1D_0541(ddl2)

ACEL:

acsn021_25810(vanG)

ACHT:

bsdcttw_22890(vanG)

QDO:	H9Q78_03830(vanG)

WHJ:	H9Q79_01750(vanG)

KIB:	RBB56_07950(vanG)

KSI:	V6984_01370(vanG)

CLE:	Clole_1511

VGU:	HYG85_23280(vanG)

ABUT:

Ami103574_02975(vanG) Ami103574_07960(vanG)

ETM:	CE91St48_02960(vanG)

EMJ:	V1225_03165(vanG)

AHAD:

FRZ06_04905(vanG)

AOE:

Clos_2860

CDF:	CD630_16260(vanG)

PDC:	CDIF630_01803(vanG)

CDC:	CD196_1549(vanG)

CDL:	CDR20291_1524(vanG)

PDF:	CD630DERM_16260(vanG)

CAD:	Curi_c05060(vanG)

SEDZ:

JYG23_10725

SEDM:

RBQ61_04740

EUC:

EC1_04100

AARG:

Aargi30884_01290(vanG)

ABSI:

A9CBEGH2_02850(vanG)

LCG:	L3BBH23_19070(vanG)

ERB:	A4V01_15880

ERM:	EYR00_02855(vanG)

CALK:

HUE98_13540(vanG)

RTS:	CE91St31_07130(vanG)

» show all

Reference

1 [PMID:1551598]

Authors

Dutka-Malen S, Molinas C, Arthur M, Courvalin P

Title

Sequence of the vanC gene of Enterococcus gallinarum BM4174 encoding a D-alanine:D-alanine ligase-related protein necessary for vancomycin resistance.

Journal

Gene 112:53-8 (1992)
DOI:10.1016/0378-1119(92)90302-6

Sequence

[ag:AAA24786]

Reference

2 [PMID:9294159]

Authors

Park IS, Lin CH, Walsh CT

Title

Bacterial resistance to vancomycin: overproduction, purification, and characterization of VanC2 from Enterococcus casseliflavus as a D-Ala-D-Ser ligase.

Journal

Proc Natl Acad Sci U S A 94:10040-4 (1997)
DOI:10.1073/pnas.94.19.10040

Reference

3 [PMID:10471558]

Authors

Fines M, Perichon B, Reynolds P, Sahm DF, Courvalin P

Title

VanE, a new type of acquired glycopeptide resistance in Enterococcus faecalis BM4405.

Journal

Antimicrob Agents Chemother 43:2161-4 (1999)
DOI:10.1128/AAC.43.9.2161

Reference

4 [PMID:14617152]

Authors

Depardieu F, Bonora MG, Reynolds PE, Courvalin P

Title

The vanG glycopeptide resistance operon from Enterococcus faecalis revisited.

Journal

Mol Microbiol 50:931-48 (2003)
DOI:10.1046/j.1365-2958.2003.03737.x

Reference

5 [PMID:19216682]

Authors

Watanabe S, Kobayashi N, Quinones D, Hayakawa S, Nagashima S, Uehara N, Watanabe N

Title

Genetic diversity of the low-level vancomycin resistance gene vanC-2/vanC-3 and identification of a novel vanC subtype (vanC-4) in Enterococcus casseliflavus.

Journal

Microb Drug Resist 15:1-9 (2009)
DOI:10.1089/mdr.2009.0856

Other DBs

ExplorEnz - The Enzyme Database:

6.3.2.35

IUBMB Enzyme Nomenclature:

6.3.2.35

ExPASy - ENZYME nomenclature database:

6.3.2.35

BRENDA, the Enzyme Database:

6.3.2.35

LinkDB

DBGET integrated database retrieval system