MGLP_BAC25
ID MGLP_BAC25 Reviewed; 250 AA.
AC P82597; Q7M0R0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Thermostable monoacylglycerol lipase;
DE Short=MGLP;
DE Short=bMGL;
DE EC=3.1.1.23;
OS Bacillus sp. (strain H-257).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=129908;
RN [1] {ECO:0000312|PIR:JC7669}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11226879; DOI=10.1093/oxfordjournals.jbchem.a002870;
RA Kitaura S., Suzuki K., Imamura S.;
RT "Monoacylglycerol lipase from moderately thermophilic Bacillus sp. strain
RT H-257: molecular cloning, sequencing, and expression in Escherichia coli of
RT the gene.";
RL J. Biochem. 129:397-402(2001).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-17, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=10731713; DOI=10.1093/oxfordjournals.jbchem.a022623;
RA Imamura S., Kitaura S.;
RT "Purification and characterization of a monoacylglycerol lipase from the
RT moderately thermophilic Bacillus sp. H-257.";
RL J. Biochem. 127:419-425(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH
RP INHIBITOR PMSF, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND
RP ACTIVE SITE.
RC STRAIN=H-257;
RX PubMed=22561231; DOI=10.1016/j.bbalip.2012.04.006;
RA Rengachari S., Bezerra G.A., Riegler-Berket L., Gruber C.C., Sturm C.,
RA Taschler U., Boeszoermenyi A., Dreveny I., Zimmermann R., Gruber K.,
RA Oberer M.;
RT "The structure of monoacylglycerol lipase from Bacillus sp. H257 reveals
RT unexpected conservation of the cap architecture between bacterial and human
RT enzymes.";
RL Biochim. Biophys. Acta 1821:1012-1021(2012).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF WILD-TYPE AND MUTANT ASN-196 IN
RP COMPLEXES WITH SUBSTRATE AND SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, ACTIVE
RP SITE, SITE, AND MUTAGENESIS OF ILE-145 AND ASP-196.
RC STRAIN=H-257;
RX PubMed=24014019; DOI=10.1074/jbc.m113.491415;
RA Rengachari S., Aschauer P., Schittmayer M., Mayer N., Gruber K.,
RA Breinbauer R., Birner-Gruenberger R., Dreveny I., Oberer M.;
RT "Conformational plasticity and ligand binding of bacterial monoacylglycerol
RT lipase.";
RL J. Biol. Chem. 288:31093-31104(2013).
CC -!- FUNCTION: Hydrolyzes monoacylglycerols, with the highest activity
CC occurring with 1-monolauroylglycerol. {ECO:0000269|PubMed:10731713}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000269|PubMed:10731713,
CC ECO:0000269|PubMed:22561231, ECO:0000269|PubMed:24014019};
CC -!- ACTIVITY REGULATION: Not inhibited by cholate, but slightly inhibited
CC by triton X-100 and deoxycholate. Completely inhibited by PMSF
CC (phenylmethylsulfonyl fluoride) at a concentration of 200 uM.
CC {ECO:0000269|PubMed:10731713, ECO:0000269|PubMed:22561231}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-8.;
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10731713,
CC ECO:0000269|PubMed:22561231}.
CC -!- MISCELLANEOUS: This lipase is not secreted extracellularly as other
CC bacterial lipases. {ECO:0000269|PubMed:10731713}.
CC -!- SIMILARITY: Belongs to the lipase/esterase LIP3/BchO family.
CC {ECO:0000305}.
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DR PIR; JC7669; JC7669.
DR PDB; 3RLI; X-ray; 1.85 A; A=1-250.
DR PDB; 3RM3; X-ray; 1.20 A; A=1-250.
DR PDB; 4KE6; X-ray; 2.80 A; A/B/C/D/E/F=1-250.
DR PDB; 4KE7; X-ray; 1.70 A; A/B=1-250.
DR PDB; 4KE8; X-ray; 1.85 A; A/B/C/D=1-250.
DR PDB; 4KE9; X-ray; 2.20 A; A/B/C/D=3-250.
DR PDB; 4KEA; X-ray; 1.70 A; A/B/C/D/E/F=1-250.
DR PDB; 4LHE; X-ray; 1.96 A; A/B=1-250.
DR PDBsum; 3RLI; -.
DR PDBsum; 3RM3; -.
DR PDBsum; 4KE6; -.
DR PDBsum; 4KE7; -.
DR PDBsum; 4KE8; -.
DR PDBsum; 4KE9; -.
DR PDBsum; 4KEA; -.
DR PDBsum; 4LHE; -.
DR AlphaFoldDB; P82597; -.
DR SMR; P82597; -.
DR ESTHER; bac25-mglp; CarbLipBact_2.
DR BRENDA; 3.1.1.23; 691.
DR GO; GO:0047372; F:acylglycerol lipase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012354; Esterase_lipase.
DR InterPro; IPR022742; Hydrolase_4.
DR Pfam; PF12146; Hydrolase_4; 1.
DR PIRSF; PIRSF017388; Esterase_lipase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Serine esterase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10731713"
FT CHAIN 2..250
FT /note="Thermostable monoacylglycerol lipase"
FT /id="PRO_0000207072"
FT ACT_SITE 97
FT /note="Nucleophile"
FT ACT_SITE 196
FT /note="Charge relay system"
FT ACT_SITE 226
FT /note="Charge relay system"
FT BINDING 29
FT /ligand="substrate"
FT BINDING 98
FT /ligand="substrate"
FT SITE 145
FT /note="Important for substrate specificity"
FT MUTAGEN 145
FT /note="I->G: 18% reduction in hydrolase activity for both
FT 1-lauroylglycerol (1-LG) and 1-oleoylglycerol (1-OG)."
FT /evidence="ECO:0000269|PubMed:24014019"
FT MUTAGEN 145
FT /note="I->S: 62% and 38% reduction in hydrolase activity
FT for 1-oleoylglycerol and 1-lauroylglycerol, respectively."
FT /evidence="ECO:0000269|PubMed:24014019"
FT MUTAGEN 196
FT /note="D->N: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:24014019"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3RM3"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:3RM3"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:3RM3"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:3RM3"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3RM3"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4KEA"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:3RM3"
FT HELIX 70..85
FT /evidence="ECO:0007829|PDB:3RM3"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:3RM3"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:3RM3"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:3RM3"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:3RM3"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:4KEA"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:3RM3"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:3RM3"
FT HELIX 164..179
FT /evidence="ECO:0007829|PDB:3RM3"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:3RM3"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:3RM3"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:3RM3"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:3RM3"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:3RM3"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3RM3"
FT HELIX 234..248
FT /evidence="ECO:0007829|PDB:3RM3"
SQ SEQUENCE 250 AA; 27359 MW; 6D315EDF65A15AAE CRC64;
MSEQYPVLSG AEPFYAENGP VGVLLVHGFT GTPHSMRPLA EAYAKAGYTV CLPRLKGHGT
HYEDMERTTF HDWVASVEEG YGWLKQRCQT IFVTGLSMGG TLTLYLAEHH PDICGIVPIN
AAVDIPAIAA GMTGGGELPR YLDSIGSDLK NPDVKELAYE KTPTASLLQL ARLMAQTKAK
LDRIVCPALI FVSDEDHVVP PGNADIIFQG ISSTEKEIVR LRNSYHVATL DYDQPMIIER
SLEFFAKHAG
