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

Alpha-maltose-1-phosphate synthase (M1P synthase) (EC 2.4.1.342) (ADP-alpha-D-glucose:alpha-D-glucose-1-phosphate 4-alpha-D-glucosyltransferase) (M1P-producing glucosyltransferase)

 GLGM_MYCTU              Reviewed;         387 AA.
P9WMZ1; L0T8Z4; O05313; Q7D8L6;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
28-MAR-2018, entry version 26.
RecName: Full=Alpha-maltose-1-phosphate synthase {ECO:0000303|PubMed:27513637};
Short=M1P synthase {ECO:0000303|PubMed:27513637};
EC=2.4.1.342 {ECO:0000269|PubMed:27513637};
AltName: Full=ADP-alpha-D-glucose:alpha-D-glucose-1-phosphate 4-alpha-D-glucosyltransferase {ECO:0000305|PubMed:27513637};
AltName: Full=M1P-producing glucosyltransferase {ECO:0000303|PubMed:27513637};
Name=glgM {ECO:0000303|PubMed:27513637}; Synonyms=glgA;
OrderedLocusNames=Rv1212c;
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]
FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18808383; DOI=10.1111/j.1365-2958.2008.06445.x;
Sambou T., Dinadayala P., Stadthagen G., Barilone N., Bordat Y.,
Constant P., Levillain F., Neyrolles O., Gicquel B., Lemassu A.,
Daffe M., Jackson M.;
"Capsular glucan and intracellular glycogen of Mycobacterium
tuberculosis: biosynthesis and impact on the persistence in mice.";
Mol. Microbiol. 70:762-774(2008).
[3]
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).
[4]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
DISRUPTION PHENOTYPE, ENZYME REGULATION, PATHWAY, AND SUBSTRATE
SPECIFICITY.
PubMed=27513637; DOI=10.1371/journal.ppat.1005768;
Koliwer-Brandl H., Syson K., van de Weerd R., Chandra G.,
Appelmelk B., Alber M., Ioerger T.R., Jacobs W.R. Jr., Geurtsen J.,
Bornemann S., Kalscheuer R.;
"Metabolic network for the biosynthesis of intra- and extracellular
alpha-glucans required for virulence of Mycobacterium tuberculosis.";
PLoS Pathog. 12:E1005768-E1005768(2016).
-!- FUNCTION: Involved in the biosynthesis of the maltose-1-phosphate
(M1P) building block required for alpha-glucan production by the
key enzyme GlgE (PubMed:18808383, PubMed:27513637). Catalyzes the
formation of an alpha-1,4 linkage between glucose from ADP-glucose
and glucose 1-phosphate (G1P) to yield maltose-1-phosphate (M1P)
(PubMed:27513637). Also able to catalyze the elongation of the
non-reducing ends of glycogen, maltodextrin and maltoheptaose
using ADP-glucose as sugar donor, however the rate of the reaction
appears to be too low to be physiologically relevant
(PubMed:27513637). GlgM is also able to use UDP-glucose as sugar
donor with G1P, however, it is less efficient than with ADP-
glucose (PubMed:27513637). UDP-glucose is not used as sugar donor
when glycogen is used as acceptor (PubMed:27513637).
{ECO:0000269|PubMed:18808383, ECO:0000269|PubMed:27513637}.
-!- CATALYTIC ACTIVITY: ADP-alpha-D-glucose + alpha-D-glucose-1-
phosphate = ADP + alpha-maltose-1-phosphate.
{ECO:0000269|PubMed:27513637}.
-!- ENZYME REGULATION: Inhibited at high G1P concentrations.
{ECO:0000269|PubMed:27513637}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.046 mM for ADP-glucose (with 4 mM of G1P)
{ECO:0000269|PubMed:27513637};
KM=0.063 mM for ADP-glucose (with 2.5 mM of G1P)
{ECO:0000269|PubMed:27513637};
KM=0.121 mM for ADP-glucose (with 1 mM of G1P)
{ECO:0000269|PubMed:27513637};
KM=0.145 mM for ADP-glucose (with 0.25 mM of G1P)
{ECO:0000269|PubMed:27513637};
KM=0.4 mM for alpha-glucan {ECO:0000269|PubMed:27513637};
KM=0.695 mM for G1P (with 4 mM of ADP-glucose)
{ECO:0000269|PubMed:27513637};
KM=0.816 mM for G1P (with 0.1 mM of ADP-glucose)
{ECO:0000269|PubMed:27513637};
KM=0.9 mM for rabbit liver glycogen
{ECO:0000269|PubMed:27513637};
KM=1.290 mM for G1P (with 0.5 mM of ADP-glucose)
{ECO:0000269|PubMed:27513637};
Vmax=136 umol/min/mg enzyme toward G1P (with 0.5 mM of ADP-
glucose) {ECO:0000269|PubMed:27513637};
Vmax=113 umol/min/mg enzyme toward G1P (with 4 mM of ADP-
glucose) {ECO:0000269|PubMed:27513637};
Vmax=54.2 umol/min/mg enzyme toward G1P (with 0.1 mM of ADP-
glucose) {ECO:0000269|PubMed:27513637};
Vmax=40.5 umol/min/mg enzyme toward ADP-glucose (with 1 mM of
G1P) {ECO:0000269|PubMed:27513637};
Vmax=27.7 umol/min/mg enzyme toward ADP-glucose (with 0.25 mM of
G1P) {ECO:0000269|PubMed:27513637};
Vmax=27.5 umol/min/mg enzyme toward ADP-glucose (with 2.5 mM of
G1P) {ECO:0000269|PubMed:27513637};
Vmax=21.4 umol/min/mg enzyme toward ADP-glucose (with 4 mM of
G1P) {ECO:0000269|PubMed:27513637};
Vmax=0.12 umol/min/mg enzyme with rabbit liver glycogen as
substrate {ECO:0000269|PubMed:27513637};
Vmax=0.02 umol/min/mg enzyme with alpha-glucan as substrate
{ECO:0000269|PubMed:27513637};
Note=Kcat is 97.9 sec(-1) for G1P as substrate (with 0.5 mM of
ADP-glucose). Kcat is 80.6 sec(-1) for G1P as substrate (with 4
mM of ADP-glucose). Kcat is 39 sec(-1) for G1P as substrate
(with 0.1 mM of ADP-glucose). Kcat is 29.2 sec(-1) for ADP-
glucose as substrate (with 1 mM of G1P). Kcat is 20 sec(-1) for
ADP-glucose as substrate (with 0.25 mM of G1P). Kcat is 19.8
sec(-1) for ADP-glucose as substrate (with 2.5 mM of G1P). Kcat
is 15.4 sec(-1) for ADP-glucose as substrate (with 4 mM of G1P).
Kcat is 0.09 sec(-1) for rabbit liver glycogen as substrate.
Kcat is 0.014 sec(-1) for alpha-glucan as substrate.
{ECO:0000269|PubMed:27513637};
-!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
{ECO:0000269|PubMed:18808383, ECO:0000269|PubMed:27513637}.
-!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
{ECO:0000269|PubMed:18808383, ECO:0000269|PubMed:27513637}.
-!- DISRUPTION PHENOTYPE: Inactivation of glgM affects the production
of extracellular alpha-glucan (two-fold reduction), but not that
of intracellular glycogen and 6-O-methylglucosyl
lipopolysaccharides (MGLP) (PubMed:18808383, PubMed:27513637).
Cells lacking this gene are also impaired in their ability to
persist in both the spleen and the lungs of mice
(PubMed:18808383). Combined inactivation of both glgM and ostA is
lethal, potentially due to accumulation of toxic levels of ADP-
glucose (PubMed:27513637). Combined inactivation of both glgM and
treS results in absence of alpha-glucan (PubMed:27513637).
{ECO:0000269|PubMed:18808383, ECO:0000269|PubMed:27513637}.
-!- MISCELLANEOUS: Maltose-1-phosphate (M1P) is generated by two
alternative routes: the TreS-Pep2 branch and the GlgC-GlgM branch,
however it seems that TreS-Pep2 branch provides most of M1P for
the GlgE pathway in M.tuberculosis. {ECO:0000269|PubMed:27513637}.
-!- MISCELLANEOUS: Attempts to disrupt both the Rv3032 gene and glgA
in order to create a mutant simultaneously deficient in both
alpha-1,4-glucosyltransferases turned out to be unsuccessful.
Thus, M.tuberculosis H37Rv requires a functional copy of at least
one of these two genes for growth. {ECO:0000269|PubMed:18808383}.
-!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL123456; CCP43968.1; -; Genomic_DNA.
PIR; B70610; B70610.
RefSeq; NP_215728.1; NC_000962.3.
RefSeq; WP_003898773.1; NZ_KK339370.1.
ProteinModelPortal; P9WMZ1; -.
SMR; P9WMZ1; -.
STRING; 83332.Rv1212c; -.
PaxDb; P9WMZ1; -.
EnsemblBacteria; CCP43968; CCP43968; Rv1212c.
GeneID; 887805; -.
KEGG; mtu:Rv1212c; -.
TubercuList; Rv1212c; -.
eggNOG; ENOG4107QPH; Bacteria.
eggNOG; COG0438; LUCA.
KO; K16148; -.
OMA; LLHGIPH; -.
PhylomeDB; P9WMZ1; -.
BioCyc; MetaCyc:G185E-5382-MONOMER; -.
UniPathway; UPA00164; -.
UniPathway; UPA00934; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IBA:GO_Central.
GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009250; P:glucan biosynthetic process; IMP:MTBBASE.
GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
InterPro; IPR001296; Glyco_trans_1.
InterPro; IPR028098; Glyco_trans_4-like_N.
InterPro; IPR011875; M1P_synthase.
Pfam; PF13439; Glyco_transf_4; 1.
Pfam; PF00534; Glycos_transf_1; 1.
TIGRFAMs; TIGR02149; glgA_Coryne; 1.
1: Evidence at protein level;
Capsule biogenesis/degradation; Carbohydrate metabolism;
Complete proteome; Glycosyltransferase; Reference proteome;
Transferase.
CHAIN 1 387 Alpha-maltose-1-phosphate synthase.
/FTId=PRO_0000413978.
SEQUENCE 387 AA; 41533 MW; BC4C4B66980BAAFF CRC64;
MRVAMLTREY PPEVYGGAGV HVTELVAYLR RLCAVDVHCM GAPRPGAFAY RPDPRLGSAN
AALSTLSADL VMANAASAAT VVHSHTWYTA LAGHLAAILY DIPHVLTAHS LEPLRPWKKE
QLGGGYQVST WVEQTAVLAA NAVIAVSSAM RNDMLRVYPS LDPNLVHVIR NGIDTETWYP
AGPARTGSVL AELGVDPNRP MAVFVGRITR QKGVVHLVTA AHRFRSDVQL VLCAGAADTP
EVADEVRVAV AELARNRTGV FWIQDRLTIG QLREILSAAT VFVCPSVYEP LGIVNLEAMA
CATAVVASDV GGIPEVVADG ITGSLVHYDA DDATGYQARL AEAVNALVAD PATAERYGHA
GRQRCIQEFS WAYIAEQTLD IYRKVCA


Related products :

Catalog number Product name Quantity


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur