GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanine:D-alanine ligase) (D-alanylalanine synthetase)

 DDL_MYCTU               Reviewed;         373 AA.
P9WP31; L0TBF6; P95114;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
13-FEB-2019, entry version 31.
RecName: Full=D-alanine--D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00047};
EC=6.3.2.4 {ECO:0000255|HAMAP-Rule:MF_00047, ECO:0000269|PubMed:20956591, ECO:0000269|PubMed:23286234};
AltName: Full=D-Ala-D-Ala ligase {ECO:0000255|HAMAP-Rule:MF_00047};
AltName: Full=D-alanine:D-alanine ligase {ECO:0000303|PubMed:20956591, ECO:0000303|PubMed:23286234};
AltName: Full=D-alanylalanine synthetase {ECO:0000255|HAMAP-Rule:MF_00047};
Name=ddl {ECO:0000255|HAMAP-Rule:MF_00047,
ECO:0000303|PubMed:20956591, ECO:0000303|PubMed:23286234};
Synonyms=ddlA; OrderedLocusNames=Rv2981c; ORFNames=MTCY349.06;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[3]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
REGULATION, KINETIC MECHANISM, AND PATHWAY.
PubMed=23286234; DOI=10.1111/febs.12108;
Prosser G.A., de Carvalho L.P.;
"Kinetic mechanism and inhibition of Mycobacterium tuberculosis D-
alanine:D-alanine ligase by the antibiotic D-cycloserine.";
FEBS J. 280:1150-1166(2013).
[4]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
ACTIVITY REGULATION, SUBUNIT, AND PATHWAY.
STRAIN=H37Rv;
PubMed=20956591; DOI=10.1128/AAC.00558-10;
Bruning J.B., Murillo A.C., Chacon O., Barletta R.G.,
Sacchettini J.C.;
"Structure of the Mycobacterium tuberculosis D-alanine:D-alanine
ligase, a target of the antituberculosis drug D-cycloserine.";
Antimicrob. Agents Chemother. 55:291-301(2011).
-!- FUNCTION: Catalyzes the ATP-driven ligation of two D-alanine
molecules to form the D-alanyl-D-alanine dipeptide. This molecule
is a key building block in peptidoglycan biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_00047, ECO:0000269|PubMed:20956591,
ECO:0000269|PubMed:23286234}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) +
phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416,
ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4;
Evidence={ECO:0000255|HAMAP-Rule:MF_00047,
ECO:0000269|PubMed:20956591, ECO:0000269|PubMed:23286234};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000250};
-!- ACTIVITY REGULATION: Is inhibited by the antituberculous drug D-
cycloserine (DCS), which is a structural analog of D-alanine
(PubMed:20956591, PubMed:23286234). Is activated by K(+)
(PubMed:23286234). {ECO:0000269|PubMed:20956591,
ECO:0000269|PubMed:23286234}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.075 mM for D-Ala (first D-Ala binding site) (at pH 7.3)
{ECO:0000269|PubMed:23286234};
KM=3.6 mM for D-Ala (second D-Ala binding site) (at pH 7.3)
{ECO:0000269|PubMed:23286234};
KM=0.31 mM for ATP (at pH 7.3) {ECO:0000269|PubMed:23286234};
Note=kcat is 9.7 sec(-1) (at pH 7.3).
{ECO:0000269|PubMed:23286234};
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_00047, ECO:0000305|PubMed:20956591,
ECO:0000305|PubMed:23286234}.
-!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:20956591}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00047}.
-!- MISCELLANEOUS: Follows an ordered ter-ter mechanism. ATP is the
first substrate to bind and is necessary for subsequent binding of
D-alanine or DCS. ADP is the final product to dissociate.
{ECO:0000269|PubMed:23286234}.
-!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
{ECO:0000255|HAMAP-Rule:MF_00047}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AL123456; CCP45786.1; -; Genomic_DNA.
PIR; B70673; B70673.
RefSeq; NP_217497.1; NC_000962.3.
RefSeq; WP_003912011.1; NZ_NVQJ01000099.1.
PDB; 3LWB; X-ray; 2.10 A; A/B=1-373.
PDBsum; 3LWB; -.
ProteinModelPortal; P9WP31; -.
SMR; P9WP31; -.
STRING; 83332.Rv2981c; -.
ChEMBL; CHEMBL2030; -.
PaxDb; P9WP31; -.
EnsemblBacteria; CCP45786; CCP45786; Rv2981c.
GeneID; 888415; -.
KEGG; mtu:Rv2981c; -.
TubercuList; Rv2981c; -.
eggNOG; ENOG4105CPF; Bacteria.
eggNOG; COG1181; LUCA.
KO; K01921; -.
OMA; YETKYTE; -.
PhylomeDB; P9WP31; -.
BioCyc; MetaCyc:G185E-7236-MONOMER; -.
BioCyc; MTBH37RV:G185E-7236-MONOMER; -.
UniPathway; UPA00219; -.
PRO; PR:P9WP31; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IDA:MTBBASE.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:MTBBASE.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
Gene3D; 3.30.1490.20; -; 1.
HAMAP; MF_00047; Dala_Dala_lig; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR000291; D-Ala_lig_Van_CS.
InterPro; IPR005905; D_ala_D_ala.
InterPro; IPR011095; Dala_Dala_lig_C.
InterPro; IPR011127; Dala_Dala_lig_N.
InterPro; IPR016185; PreATP-grasp_dom_sf.
Pfam; PF07478; Dala_Dala_lig_C; 1.
Pfam; PF01820; Dala_Dala_lig_N; 1.
PIRSF; PIRSF039102; Ddl/VanB; 1.
SUPFAM; SSF52440; SSF52440; 1.
TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell shape;
Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
Peptidoglycan synthesis; Reference proteome.
CHAIN 1 373 D-alanine--D-alanine ligase.
/FTId=PRO_0000177844.
DOMAIN 156 363 ATP-grasp. {ECO:0000255|HAMAP-
Rule:MF_00047}.
NP_BIND 184 239 ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
METAL 318 318 Magnesium or manganese 1.
{ECO:0000255|HAMAP-Rule:MF_00047}.
METAL 330 330 Magnesium or manganese 1.
{ECO:0000255|HAMAP-Rule:MF_00047}.
METAL 330 330 Magnesium or manganese 2.
{ECO:0000255|HAMAP-Rule:MF_00047}.
METAL 332 332 Magnesium or manganese 2.
{ECO:0000255|HAMAP-Rule:MF_00047}.
STRAND 11 18 {ECO:0000244|PDB:3LWB}.
HELIX 26 37 {ECO:0000244|PDB:3LWB}.
TURN 40 42 {ECO:0000244|PDB:3LWB}.
STRAND 43 50 {ECO:0000244|PDB:3LWB}.
STRAND 56 59 {ECO:0000244|PDB:3LWB}.
HELIX 103 108 {ECO:0000244|PDB:3LWB}.
STRAND 111 115 {ECO:0000244|PDB:3LWB}.
HELIX 126 134 {ECO:0000244|PDB:3LWB}.
STRAND 138 141 {ECO:0000244|PDB:3LWB}.
HELIX 143 150 {ECO:0000244|PDB:3LWB}.
HELIX 152 161 {ECO:0000244|PDB:3LWB}.
STRAND 169 172 {ECO:0000244|PDB:3LWB}.
HELIX 181 187 {ECO:0000244|PDB:3LWB}.
STRAND 191 197 {ECO:0000244|PDB:3LWB}.
TURN 200 203 {ECO:0000244|PDB:3LWB}.
STRAND 205 207 {ECO:0000244|PDB:3LWB}.
HELIX 210 212 {ECO:0000244|PDB:3LWB}.
HELIX 213 221 {ECO:0000244|PDB:3LWB}.
STRAND 225 231 {ECO:0000244|PDB:3LWB}.
STRAND 234 244 {ECO:0000244|PDB:3LWB}.
STRAND 250 252 {ECO:0000244|PDB:3LWB}.
STRAND 256 259 {ECO:0000244|PDB:3LWB}.
STRAND 266 271 {ECO:0000244|PDB:3LWB}.
HELIX 273 277 {ECO:0000244|PDB:3LWB}.
STRAND 283 287 {ECO:0000244|PDB:3LWB}.
HELIX 292 308 {ECO:0000244|PDB:3LWB}.
STRAND 313 322 {ECO:0000244|PDB:3LWB}.
STRAND 325 334 {ECO:0000244|PDB:3LWB}.
HELIX 342 349 {ECO:0000244|PDB:3LWB}.
HELIX 354 367 {ECO:0000244|PDB:3LWB}.
SEQUENCE 373 AA; 39710 MW; FD7838E8B7526B53 CRC64;
MSANDRRDRR VRVAVVFGGR SNEHAISCVS AGSILRNLDS RRFDVIAVGI TPAGSWVLTD
ANPDALTITN RELPQVKSGS GTELALPADP RRGGQLVSLP PGAGEVLESV DVVFPVLHGP
YGEDGTIQGL LELAGVPYVG AGVLASAVGM DKEFTKKLLA ADGLPVGAYA VLRPPRSTLH
RQECERLGLP VFVKPARGGS SIGVSRVSSW DQLPAAVARA RRHDPKVIVE AAISGRELEC
GVLEMPDGTL EASTLGEIRV AGVRGREDSF YDFATKYLDD AAELDVPAKV DDQVAEAIRQ
LAIRAFAAID CRGLARVDFF LTDDGPVINE INTMPGFTTI SMYPRMWAAS GVDYPTLLAT
MIETTLARGV GLH


Related products :

Catalog number Product name Quantity
10-663-45328 Alanine tRNA Ligase (PL-12) Human - EC 6.1.1.7; Alanine--tRNA ligase; AlaRS; NY-REN-42 antigen N_A 0.02 mg
10-663-45328 Alanine tRNA Ligase (PL-12) Human - EC 6.1.1.7; Alanine--tRNA ligase; AlaRS; NY-REN-42 antigen N_A 0.005 mg
10-663-45328 Alanine tRNA Ligase (PL-12) Human - EC 6.1.1.7; Alanine--tRNA ligase; AlaRS; NY-REN-42 antigen N_A 1 mg
EIAAB40675 Aars,Alanine--tRNA ligase,Alanyl-tRNA synthetase, cytoplasmic,AlaRS,Mouse,Mus musculus
EIAAB40674 Aars,Alanine--tRNA ligase,Alanyl-tRNA synthetase, cytoplasmic,AlaRS,Rat,Rattus norvegicus
EIAAB40678 Aars2,Alanine--tRNA ligase,Alanyl-tRNA synthetase, mitochondrial,AlaRS,Rat,Rattus norvegicus,rCG_43500
70-600 anti-AlaRS (Alanine-tRNA Ligase) antibody 100 ul
EIAAB40676 Aars2,Aarsl,Alanine--tRNA ligase,Alanyl-tRNA synthetase, mitochondrial,AlaRS,Gm89,Kiaa1270,Mouse,Mus musculus
EIAAB40677 AARS2,AARSL,Alanine--tRNA ligase,Alanyl-tRNA synthetase, mitochondrial,AlaRS,Homo sapiens,Human,KIAA1270
70-600 anti-AlaRS (Alanine-tRNA Ligase) antibody Antibodies 100 ul
EIAAB40673 AARS,Alanine--tRNA ligase,Alanyl-tRNA synthetase, cytoplasmic,AlaRS,Homo sapiens,Human,Renal carcinoma antigen NY-REN-42
70-600 anti-AlaRS (Alanine-tRNA Ligase) antibody Antibodies DNA Repair_Recombination 100 ul
30-489 GPT and GPT2 (EC 2.6.1.2), also known as alanine transaminases, are pyridoxal enzymes that catalyze the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. By 0.05 mg
26-367 GPT and GPT2 (EC 2.6.1.2), also known as alanine transaminases, are pyridoxal enzymes that catalyze the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. By 0.05 mg
9000-86-6 Alanine aminotransferase Alanine aminotransfera 1g
7764-95-6 N-tert-Butoxycarbonyl-D-alanine BOC-D-Alanine 1g
125814-23-5 Z-L-Alanine N-carboxyanhydride Z-L-Alanine N-carboxya 1g
EALA-100 EnzyChrom™ L-Alanine Assay Kit, Quantitative assay of L-Alanine by colorimetric (570nm) or fluorimetric (530nm_590nm) methods 100Tests
EALT-100 EnzyChrom™ Alanine Transaminase Assay Kit, Quantitative determination of Alanine transaminase activity at 340nm 100Tests
orb62010 D-Alanine D-Alanine For research use only. 400 g
EALA-100 EnzyChrom™ L-Alanine Assay Kit, Quantitative assay of L-Alanine by colorimetric (570nm) or fluorimetric (530nm_590nm) methods. Procedure 60 min. Kit size 100 tests. Detection limit 0.4 µM. Shelf li 100tests
EALT-100 EnzyChrom™ Alanine Transaminase Assay Kit, Quantitative determination of Alanine transaminase activity at 340nm. Procedure 10 min. Kit size 100 tests. Detection limit 2 U_L. Shelf life 3 months. S 100tests
3403-35-6 D_Phenyl alanine tert_butyl ester hydroch D_Phenyl alanine tert_b 1g
55535-58-5 N-dodecanoyl-alanine mono sodium salt N-dodecanoyl-alanine 1g
13033-84-6 R-Phenyl Alanine Methyl Ester HCL R-Phenyl Alanine Meth 1g

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP104: Alanine and aspartate metabolism
WP106: Alanine and aspartate metabolism
WP1617: Alanine, aspartate and glutamate metabolism
WP1628: beta-Alanine metabolism
WP1641: D-Alanine metabolism
WP2185: Purine metabolism
WP2207: β-alanine biosynthesis
WP240: Alanine and aspartate metabolism
WP1097: Non-homologous end joining
WP1201: Non-homologous end joining
WP1208: Non-homologous end joining
WP1222: Non-homologous end joining
WP1242: Non-homologous end joining
WP1277: Non-homologous end joining
WP1324: Non-homologous end joining
WP1570: Non-homologous end joining
WP1625: Base excision repair
WP1672: Mismatch repair
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair
WP1996: Linoleate Biosynthesis
WP296: TCA Cycle - biocyc
WP438: Non-homologous end joining
WP739: Non-homologous end joining
WP753: Non-homologous end joining

Related Genes :
[ddl ddlA Rv2981c MTCY349.06] D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanine:D-alanine ligase) (D-alanylalanine synthetase)
[ddlB ddl b0092 JW0090] D-alanine--D-alanine ligase B (EC 6.3.2.4) (D-Ala-D-Ala ligase B) (D-alanylalanine synthetase B)
[murC/ddl CT_762] Bifunctional enzyme MurC/Ddl [Includes: UDP-N-acetylmuramate--L-alanine ligase (EC 6.3.2.8) (UDP-N-acetylmuramoyl-L-alanine synthetase); D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)]
[murC/ddl TC_0143] Bifunctional enzyme MurC/Ddl [Includes: UDP-N-acetylmuramate--L-alanine ligase (EC 6.3.2.8) (UDP-N-acetylmuramoyl-L-alanine synthetase); D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)]
[bacD ywfE BSU37710 ipa-83d] Alanine--anticapsin ligase (EC 6.3.2.49) (ATP-dependent dipeptide ligase) (Bacilysin synthetase) (L-Ala-L-amino acid dipeptide ligase) (L-alanine--L-anticapsin ligase) (L-amino acid ligase) (Lal)
[murC/ddl CPn_0905 CP_0961 CpB0937] Bifunctional enzyme MurC/Ddl [Includes: UDP-N-acetylmuramate--L-alanine ligase (EC 6.3.2.8) (UDP-N-acetylmuramoyl-L-alanine synthetase); D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)]
[murC/ddlA CCA_00863] Bifunctional enzyme MurC/Ddl [Includes: UDP-N-acetylmuramate--L-alanine ligase (EC 6.3.2.8) (UDP-N-acetylmuramoyl-L-alanine synthetase); D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)]
[ddlA STM0380] D-alanine--D-alanine ligase A (EC 6.3.2.4) (D-Ala-D-Ala ligase A) (D-alanylalanine synthetase A)
[ddlA b0381 JW0372] D-alanine--D-alanine ligase A (EC 6.3.2.4) (D-Ala-D-Ala ligase A) (D-alanylalanine synthetase A)
[vanX] D-alanyl-D-alanine dipeptidase (D-Ala-D-Ala dipeptidase) (EC 3.4.13.22) (Vancomycin B-type resistance protein VanX)
[vanA] Vancomycin/teicoplanin A-type resistance protein VanA (EC 6.1.2.1) (D-alanine--D-lactate ligase) (VanA ligase)
[ddl SPD_1484] D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)
[murE b0085 JW0083] UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (EC 6.3.2.13) (Meso-A2pm-adding enzyme) (Meso-diaminopimelate-adding enzyme) (UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase) (UDP-MurNAc-tripeptide synthetase) (UDP-N-acetylmuramyl-tripeptide synthetase)
[ddl Cla_0634] D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)
[ddlB c0110] D-alanine--D-alanine ligase B (EC 6.3.2.4) (D-Ala-D-Ala ligase B) (D-alanylalanine synthetase B)
[botD] Botulinum neurotoxin type D (BoNT/D) (Bontoxilysin-D) [Cleaved into: Botulinum neurotoxin D light chain (LC) (EC 3.4.24.69); Botulinum neurotoxin D heavy chain (HC)]
[dtd PF11_0095 PF3D7_1108200] D-aminoacyl-tRNA deacylase (DTD) (EC 3.1.1.96) (D-Tyrosyl-tRNA(Tyr) deacylase) (Gly-tRNA(Ala) deacylase) (EC 3.1.1.-) (Gly-tRNA(Gly) deacylase)
[ddlB Z0102 ECs0096] D-alanine--D-alanine ligase B (EC 6.3.2.4) (D-Ala-D-Ala ligase B) (D-alanylalanine synthetase B)
[ddl ddlB ddlB_1 ddlB_2 AGG09_09840 AXA55_09490 B1727_29425 B4U30_00905 B4U35_24790 C3483_22030 C3F39_10475 C7V41_14830 CPT10_02575 CSC88_14250 CWN54_18505 D0897_15420 DDJ63_07735 DM081_06090 DXF97_05340 DY552_01150 DZB15_21585 NCTC11679_04748 NCTC204_00769 NCTC5052_02869 NCTC5053_04321 NCTC8849_01054 NCTC9128_05386 NCTC9601_05902 NCTC9617_05375 NCTC9637_05613 NCTC9645_02971 NCTC9661_05276 PMK1_02404 SAMEA104305404_02881 SAMEA23986918_05509 SAMEA3649709_01985 SAMEA4394730_05381] D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)
[ddlB STM0130] D-alanine--D-alanine ligase B (EC 6.3.2.4) (D-Ala-D-Ala ligase B) (D-alanylalanine synthetase B)
[ddlB STY0150 t0134] D-alanine--D-alanine ligase B (EC 6.3.2.4) (D-Ala-D-Ala ligase B) (D-alanylalanine synthetase B)
[ddl ddlA SpyM3_1084] D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)
[vanB vanB2 EF_2294] Vancomycin B-type resistance protein VanB (EC 6.1.2.1) (D-alanine--D-lactate ligase) (VanB ligase)
[ddl ddlB HI_1140] D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)
[ddl ddlB BUsg_208] D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)
[ddlA ddl ddlA_1 AGG09_08580 B4U21_03005 B4U25_03320 BN49_1297 C3F39_09305 C7V41_10990 CPT10_16635 CWN54_27530 D0897_14160 DM059_03135 DM062_02650 DM081_11800 DXF97_00195 DY552_02400 NCTC1936_04634 NCTC8849_01374 NCTC9637_05299 SAMEA23986918_03029 SAMEA3649709_02130 SAMEA4364603_03016] D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)
[ddl ddlA SCO5560 SC7A1.04] D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[ddl Selsp_1818 SELSPUOL_00331] D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)
[ddl BamMC406_0490] D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)

Bibliography :
[30300845] 1-(2-Hydroxybenzoyl)-thiosemicarbazides are promising antimicrobial agents targeting d-alanine-d-alanine ligase in bacterio.
[29401644] The Biological Properties and Potential Interacting Proteins of d-Alanyl-d-alanine Ligase A from Mycobacterium tuberculosis.
[29208891] Inhibition of D-Ala:D-Ala ligase through a phosphorylated form of the antibiotic D-cycloserine.
[26894530] Structure of D-alanine-D-alanine ligase from Yersinia pestis: nucleotide phosphate recognition by the serine loop.
[26526529] d-Alanine metabolism is essential for growth and biofilm formation of Streptococcus mutans.
[26502962] The crystal structure of the D-alanine-D-alanine ligase from Acinetobacter baumannii suggests a flexible conformational change in the central domain before nucleotide binding.
[26279274] A new member of MocR/GabR-type PLP-binding regulator of D-alanyl-D-alanine ligase in Brevibacillus brevis.
[26200029] Characterization of daptomycin non-susceptible Enterococcus faecium producing urinary tract infection in a renal transplant recipient.
[24699750] Expression, crystallization and preliminary X-ray crystallographic analysis of D-alanine-D-alanine ligase from OXA-23-producing Acinetobacter baumannii K0420859.
[24440607] Crystal structures of d-alanine-d-alanine ligase from Xanthomonas oryzae pv. oryzae alone and in complex with nucleotides.
?>