LIP_STRRM
ID LIP_STRRM Reviewed; 268 AA.
AC Q93MW7;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:20931591, ECO:0000269|Ref.5};
DE AltName: Full=Diheptanoyl glycerophosphocholine esterase;
DE EC=3.1.1.-;
DE AltName: Full=Extracellular lipase;
DE AltName: Full=GDSL-like lipase;
DE AltName: Full=Palmitoyl-CoA hydrolase;
DE EC=3.1.2.2 {ECO:0000269|PubMed:20931591};
DE AltName: Full=SRL;
DE Flags: Precursor;
OS Streptomyces rimosus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1927;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 35-55; 67-76;
RP 81-90; 91-97; 98-109; 113-122; 146-152; 155-158; 181-191; 195-209; 212-223;
RP 247-254 AND 259-268.
RC STRAIN=R6;
RX PubMed=12115057; DOI=10.1007/s00203-002-0430-6;
RA Vujaklija D., Schroeder W., Abramic M., Zou P., Lescic I., Franke P.,
RA Pigac J.;
RT "A novel streptomycete lipase: cloning, sequencing and high-level
RT expression of the Streptomyces rimosus GDS(L)-lipase gene.";
RL Arch. Microbiol. 178:124-130(2002).
RN [2]
RP MASS SPECTROMETRY, AND IDENTIFICATION OF DISULFIDE BONDS.
RC STRAIN=R6;
RX PubMed=15653427; DOI=10.1515/bc.2004.148;
RA Lescic I., Zehl M., Mueller R., Vukelic B., Abramic M., Pigac J.,
RA Allmaier G., Kojic-Prodic B.;
RT "Structural characterization of extracellular lipase from Streptomyces
RT rimosus: assignment of disulfide bridge pattern by mass spectrometry.";
RL Biol. Chem. 385:1147-1156(2004).
RN [3]
RP CHARACTERIZATION OF SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INHIBITION BY PHENYLMETHYLSULPHONYL
RP FLUORIDE.
RC STRAIN=R6;
RA Abramic M., Lescic I., Korica T., Vitale L., Saenger W., Pigac J.;
RT "Purification and properties of extracellular lipase from Streptomyces
RT rimosus.";
RL Enzyme Microb. Technol. 25:522-529(1999).
RN [4]
RP FUNCTION, SUBSTRATE SPECIFICITY, TRANSESTERIFICATION ACTIVITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=R6;
RX DOI=10.1016/S0141-0229(01)00433-1;
RA Lescic I., Vukelic B., Majeric-Elenkov M., Saenger W., Abramic M.;
RT "Substrate specificity and effects of water-miscible solvents on the
RT activity and stability of extracellular lipase from Streptomyces rimosus.";
RL Enzyme Microb. Technol. 29:548-553(2001).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=R6;
RA Vujaklija D., Abramic M., Lescic I., Marsic T., Pigac J.;
RT "Streptomyces rimosus GDS(L) Lipase: production, heterologous
RT overexpression and structure-stability relationship.";
RL Food Technol. Biotechnol. 41:89-93(2003).
RN [6]
RP IDENTIFICATION OF ACTIVE SITE SERINE, MASS SPECTROMETRY, AND INHIBITION BY
RP 3,4-DICHLOROISOCOUMARIN.
RC STRAIN=R6;
RX PubMed=15578758; DOI=10.1002/jms.750;
RA Zehl M., Lescic I., Abramic M., Rizzi A., Kojic-Prodic B., Allmaier G.;
RT "Characterization of covalently inhibited extracellular lipase from
RT Streptomyces rimosus by matrix-assisted laser desorption/ionization time-
RT of-flight and matrix-assisted laser desorption/ionization quadrupole ion
RT trap reflectron time-of-flight mass spectrometry: localization of the
RT active site serine.";
RL J. Mass Spectrom. 39:1474-1483(2004).
RN [7]
RP BINDING OF THE INHIBITOR TETRAHYDROLIPSTATIN (THL) TO ACTIVE SITE SERINE.
RC STRAIN=R6;
RX PubMed=17137716; DOI=10.1016/j.bbagen.2006.10.011;
RA Asler I.L., Zehl M., Kovacic F., Mueller R., Abramic M., Allmaier G.,
RA Kojic-Prodic B.;
RT "Mass spectrometric evidence of covalently-bound tetrahydrolipstatin at the
RT catalytic serine of Streptomyces rimosus lipase.";
RL Biochim. Biophys. Acta 1770:163-170(2007).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND KINETIC
RP PARAMETERS.
RC STRAIN=R6;
RX PubMed=20931591; DOI=10.1002/cbic.201000398;
RA Lescic Asler I., Ivic N., Kovacic F., Schell S., Knorr J., Krauss U.,
RA Wilhelm S., Kojic-Prodic B., Jaeger K.E.;
RT "Probing enzyme promiscuity of SGNH hydrolases.";
RL ChemBioChem 11:2158-2167(2010).
CC -!- FUNCTION: Catalyzes the hydrolysis of p-nitrophenyl esters, alpha- and
CC beta-naphthyl esters, and triacylglycerols, with a preference for
CC medium acyl chain length (C8-C12). Shows a much higher hydrolysis rate
CC of glycerol esters of unsaturated C16 and C18 fatty acids than that of
CC their saturated counterparts, and a preference for cis double bond. Is
CC also able to hydrolyze several natural oils and Tween detergents. Also
CC displays thioesterase and phospholipase activities, towards palmitoyl-
CC coenzyme A and diheptanoyl glycerophosphocholine, respectively. Shows
CC transesterification activity of racemic 1-phenyl ethanol with vinyl
CC acetate in hexane, proceeding with partial (R)-enantioselectivity.
CC {ECO:0000269|PubMed:20931591, ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000269|PubMed:20931591, ECO:0000269|Ref.5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC Evidence={ECO:0000269|PubMed:20931591};
CC -!- ACTIVITY REGULATION: Inhibited by 3,4-dichloroisocoumarin and
CC tetrahydrolipstatin in the absence of substrate, but by
CC phenylmethylsulfonyl fluoride (PMSF) only in the presence of substrate.
CC Several water-miscible solvents enhance the lipase hydrolytic activity
CC in vitro. Tetrahydrofuran and N,N-dimethylformamide (both 50%)
CC inactivate the enzyme with t1/2 of 5 minutes and t1/2 of 2 hours,
CC respectively. {ECO:0000269|Ref.4}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|Ref.3};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius at pH 8.0.
CC {ECO:0000269|Ref.3};
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3}.
CC -!- INDUCTION: Expressed once the cells enter stationary phase, with a
CC maximum at the late stationary phase. {ECO:0000269|Ref.5}.
CC -!- MASS SPECTROMETRY: Mass=24165.87; Mass_error=1.14; Method=MALDI;
CC Note=Value for wild-type lipase.;
CC Evidence={ECO:0000269|PubMed:15653427};
CC -!- MASS SPECTROMETRY: Mass=24166.01; Mass_error=1.16; Method=MALDI;
CC Note=Value for lipase overexpressed in S.rimosus.;
CC Evidence={ECO:0000269|PubMed:15653427};
CC -!- MASS SPECTROMETRY: Mass=24166.0; Mass_error=1.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15578758};
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- CAUTION: In PubMed:17137716 the protein has been overexpressed in
CC S.lividans, where it is incorrectly processed and has 2 additional N-
CC terminal amino acids. {ECO:0000305}.
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DR EMBL; AF394224; AAK84028.1; -; Genomic_DNA.
DR RefSeq; WP_003986773.1; NZ_SADA01000186.1.
DR PDB; 5MAL; X-ray; 1.71 A; A/B=35-268.
DR PDBsum; 5MAL; -.
DR AlphaFoldDB; Q93MW7; -.
DR SMR; Q93MW7; -.
DR GeneID; 66853929; -.
DR OMA; QNSYHPN; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd01823; SEST_like; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR037460; SEST-like.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR37981; PTHR37981; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Secreted; Serine esterase; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:12115057"
FT CHAIN 35..268
FT /note="Lipase"
FT /id="PRO_0000292983"
FT ACT_SITE 44
FT /note="Nucleophile"
FT ACT_SITE 250
FT /evidence="ECO:0000305"
FT DISULFID 61..86
FT DISULFID 127..135
FT DISULFID 185..232
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:5MAL"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:5MAL"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:5MAL"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:5MAL"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:5MAL"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:5MAL"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:5MAL"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:5MAL"
FT TURN 115..119
FT /evidence="ECO:0007829|PDB:5MAL"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:5MAL"
FT HELIX 132..148
FT /evidence="ECO:0007829|PDB:5MAL"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:5MAL"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:5MAL"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:5MAL"
FT HELIX 191..214
FT /evidence="ECO:0007829|PDB:5MAL"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:5MAL"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:5MAL"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5MAL"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:5MAL"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:5MAL"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:5MAL"
SQ SEQUENCE 268 AA; 27607 MW; 7C569CD891B5CE87 CRC64;
MRLSRRAATA SALLLTPALA LFGASAAVSA PRIQATDYVA LGDSYSSGVG AGSYDSSSGS
CKRSTKSYPA LWAASHTGTR FNFTACSGAR TGDVLAKQLT PVNSGTDLVS ITIGGNDAGF
ADTMTTCNLQ GESACLARIA KARAYIQQTL PAQLDQVYDA IDSRAPAAQV VVLGYPRFYK
LGGSCAVGLS EKSRAAINAA ADDINAVTAK RAADHGFAFG DVNTTFAGHE LCSGAPWLHS
VTLPVENSYH PTANGQSKGY LPVLNSAT
