MGL2_YEAST
ID MGL2_YEAST Reviewed; 449 AA.
AC Q03649; D6W035;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Monoacylglycerol lipase {ECO:0000303|PubMed:26991558};
DE Short=MAG lipase;
DE EC=3.1.1.23 {ECO:0000269|PubMed:26991558};
GN Name=MGL2 {ECO:0000303|PubMed:26991558}; OrderedLocusNames=YMR210W;
GN ORFNames=YM8261.04;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=16361250; DOI=10.1074/jbc.m512028200;
RA Saerens S.M.G., Verstrepen K.J., Van Laere S.D., Voet A.R., Van Dijck P.,
RA Delvaux F.R., Thevelein J.M.;
RT "The Saccharomyces cerevisiae EHT1 and EEB1 genes encode novel enzymes with
RT medium-chain fatty acid ethyl ester synthesis and hydrolysis capacity.";
RL J. Biol. Chem. 281:4446-4456(2006).
RN [4]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-82, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF SER-232.
RX PubMed=26991558; DOI=10.1002/1873-3468.12136;
RA Selvaraju K., Gowsalya R., Vijayakumar R., Nachiappan V.;
RT "MGL2/YMR210w encodes a monoacylglycerol lipase in Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 590:1174-1186(2016).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=29225428; DOI=10.6026/97320630013360;
RA Manda N.K., Thunuguntla V.B.S.C., Bokka C., Singh B.J.;
RT "Ymr210wp leads to the accumulation of phospholipids and steryl esters in
RT yeast.";
RL Bioinformation 13:360-365(2017).
CC -!- FUNCTION: Converts monoacylglycerides (MAG) to free fatty acids and
CC glycerol. Has a preference for palmitoyl-MAG (PubMed:26991558). Does
CC not play a significant role in ethyl ester biosynthesis
CC (PubMed:16361250). Also possesses ester hydrolase and low but
CC persistent TAG lipase activity (PubMed:29225428).
CC {ECO:0000269|PubMed:16361250, ECO:0000269|PubMed:26991558,
CC ECO:0000269|PubMed:29225428}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000269|PubMed:26991558};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:39959, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:69081; Evidence={ECO:0000269|PubMed:26991558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39960;
CC Evidence={ECO:0000305|PubMed:26991558};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoylglycerol + H2O = glycerol + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:38363, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:75555; Evidence={ECO:0000269|PubMed:26991558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38364;
CC Evidence={ECO:0000305|PubMed:26991558};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:26991558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000305|PubMed:26991558};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25.89 uM for palmitoyl-MAG {ECO:0000269|PubMed:26991558};
CC KM=11.51 uM for p-nitrophenyl acetate {ECO:0000269|PubMed:29225428};
CC KM=7.28 uM for p-nitrophenyl butyrate {ECO:0000269|PubMed:29225428};
CC KM=13.19 uM for p-nitrophenyl palmitate
CC {ECO:0000269|PubMed:29225428};
CC Vmax=36.76 nmol/min/mg enzyme for MAG lipase activity
CC {ECO:0000269|PubMed:26991558};
CC Vmax=0.26 umol/min/mg enzyme towards p-nitrophenyl butyrate
CC {ECO:0000269|PubMed:26991558};
CC Vmax=0.18 umol/min/mg enzyme towards p-nitrophenyl acetate
CC {ECO:0000269|PubMed:26991558};
CC Vmax=0.33 umol/min/mg enzyme towards p-nitrophenyl palmitate
CC {ECO:0000269|PubMed:26991558};
CC pH dependence:
CC Optimum pH is 7.0 for MAG lipase activity. Active over a broad pH
CC range from pH 6 to pH 9 (PubMed:26991558). Optimum pH is 8.5 for p-
CC nitrophenyl palmitate and pH 7.5 for both p-nitrophenyl acetate and
CC p-nitrophenyl butyrate (PubMed:29225428).
CC {ECO:0000269|PubMed:26991558, ECO:0000269|PubMed:29225428};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius for MAG lipase activity
CC (PubMed:26991558). Optimum temperature is 45 degrees Celsius for p-
CC nitrophenyl palmitate and 30 degrees Celsius for both p-nitrophenyl
CC acetate and p-nitrophenyl butyrate (PubMed:29225428).
CC {ECO:0000269|PubMed:26991558, ECO:0000269|PubMed:29225428};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 4
CC family. {ECO:0000305}.
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DR EMBL; Z49809; CAA89925.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10109.1; -; Genomic_DNA.
DR PIR; S55092; S55092.
DR RefSeq; NP_013937.1; NM_001182717.1.
DR AlphaFoldDB; Q03649; -.
DR BioGRID; 35388; 78.
DR DIP; DIP-1964N; -.
DR IntAct; Q03649; 3.
DR MINT; Q03649; -.
DR STRING; 4932.YMR210W; -.
DR SwissLipids; SLP:000001904; -.
DR ESTHER; yeast-ym60; abh_upf0017.
DR iPTMnet; Q03649; -.
DR PaxDb; Q03649; -.
DR PRIDE; Q03649; -.
DR EnsemblFungi; YMR210W_mRNA; YMR210W; YMR210W.
DR GeneID; 855250; -.
DR KEGG; sce:YMR210W; -.
DR SGD; S000004823; MGL2.
DR VEuPathDB; FungiDB:YMR210W; -.
DR eggNOG; KOG1838; Eukaryota.
DR GeneTree; ENSGT00950000182902; -.
DR HOGENOM; CLU_032487_1_0_1; -.
DR InParanoid; Q03649; -.
DR OMA; NYCGEEG; -.
DR BioCyc; MetaCyc:G3O-32893-MON; -.
DR BioCyc; YEAST:G3O-32893-MON; -.
DR Reactome; R-SCE-1483191; Synthesis of PC.
DR PRO; PR:Q03649; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03649; protein.
DR GO; GO:0008126; F:acetylesterase activity; IBA:GO_Central.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:SGD.
DR GO; GO:0016746; F:acyltransferase activity; ISS:SGD.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:SGD.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; IGI:SGD.
DR GO; GO:0051793; P:medium-chain fatty acid catabolic process; IBA:GO_Central.
DR GO; GO:0006641; P:triglyceride metabolic process; IGI:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000952; AB_hydrolase_4_CS.
DR InterPro; IPR012020; ABHD4.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005211; Ab_hydro_YheT; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01133; UPF0017; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Isopeptide bond; Reference proteome; Serine esterase;
KW Ubl conjugation.
FT CHAIN 1..449
FT /note="Monoacylglycerol lipase"
FT /id="PRO_0000212455"
FT DOMAIN 151..392
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT MOTIF 230..234
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:P28321"
FT ACT_SITE 232
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P28321"
FT ACT_SITE 364
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P28321"
FT ACT_SITE 392
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P28321"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 232
FT /note="S->A: Abolishes MAG lipase activity."
FT /evidence="ECO:0000269|PubMed:26991558"
SQ SEQUENCE 449 AA; 51438 MW; 80B6E876DF179F10 CRC64;
MRLKELLPNF LIVHQEVPED PIAFKSTDKR ENENKEITIP ELIDTKVPEL ADGATDTLYG
LLVNGHLQTA YGSFRHFDNI YKVQYKRMII KYPHGGEGTV DFAVNGRSTK RRKVEKEYVP
TSQPVFNGNL KRRYSYYSPD DPKLNSDDAK PMLIILHGLT GGSRESYVRA IVHEITTKYD
FEACVFNARG CCYSAITTPL LYNGGWTNDI RYCVNDLRKR FPNRKFYMMG FSLGASIMTN
YLGEESDRTK IECAISVSNP FDLYNSAYFI NSTPMGSRFY SPALGHNLLR MVRNHLSTLE
ENPDFKDVIE KHLKKIRTVR QFDNLLTGPM FGYKNAEEYY KNASSYKRIP GIRTPFIALH
AQDDPIVGGD LPIDQIKSNP YTLLLETSTG GHVGWFKDRS GRRWYAEPLC RFLKIFHDEI
TVKGLKPDLE NVQLPDPNCE PIATTFRAN
