LIP_RHIOR
ID LIP_RHIOR Reviewed; 392 AA.
AC P61872; P21811; Q12237; Q5J329; Q7M4U7; Q9P312;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:8862551};
DE AltName: Full=RDL;
DE AltName: Full=Triacylglycerol lipase;
DE Short=ROL;
DE Flags: Precursor;
OS Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=64495;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 34612;
RX PubMed=1756969; DOI=10.1016/0378-1119(91)90594-2;
RA Haas M.J., Berka T.R.;
RT "Cloning, expression and characterization of a cDNA encoding a lipase from
RT Rhizopus delemar.";
RL Gene 109:107-113(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 124-128, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 4858 / DSM 853 / CBS 327.47;
RX PubMed=9765593; DOI=10.1016/s0167-4781(98)00104-3;
RA Beer H.D., McCarthy J.E.G., Bornscheuer U.T., Schmid R.D.;
RT "Cloning, expression, characterization and role of the leader sequence of a
RT lipase from Rhizopus oryzae.";
RL Biochim. Biophys. Acta 1399:173-180(1998).
RN [3]
RP PROTEIN SEQUENCE OF 96-123; 126-134; 173-209; 280-321; 327-364 AND 366-390,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8329142; DOI=10.1515/bchm3.1993.374.1-6.245;
RA Uyttenbroeck W., Hendriks D., Vriend G., de Baere I., Moens L., Scharpe S.;
RT "Molecular characterization of an extracellular acid-resistant lipase
RT produced by Rhizopus javanicus.";
RL Biol. Chem. Hoppe-Seyler 374:245-254(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 96-392, AND PROTEIN SEQUENCE OF
RP 124-144.
RX PubMed=15710378; DOI=10.1016/j.febslet.2004.12.068;
RA Sayari A., Frikha F., Miled N., Mtibaa H., Ben-Ali Y., Verger R.,
RA Gargouri Y.;
RT "N-terminal peptide of Rhizopus oryzae lipase is important for its
RT catalytic properties.";
RL FEBS Lett. 579:976-982(2005).
RN [5]
RP PROTEIN SEQUENCE OF 96-115, FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=11506890; DOI=10.1016/s0300-9084(01)01283-4;
RA Ben-Salah A., Sayari A., Verger R., Gargouri Y.;
RT "Kinetic studies of Rhizopus oryzae lipase using monomolecular film
RT technique.";
RL Biochimie 83:463-469(2001).
RN [6]
RP MUTAGENESIS OF CYS-56.
RX PubMed=8912667; DOI=10.1042/bj3190351;
RA Beer H.D., Wohlfahrt G., Schmid R.D., McCarthy J.E.G.;
RT "The folding and activity of the extracellular lipase of Rhizopus oryzae
RT are modulated by a prosequence.";
RL Biochem. J. 319:351-359(1996).
RN [7]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP TYR-151; THR-206; ALA-212; ASP-215; HIS-267; ASP-327 AND GLU-388.
RX PubMed=8862551; DOI=10.1093/protein/9.6.507;
RA Beer H.D., Wohlfahrt G., McCarthy J.E.G., Schomburg D., Schmid R.D.;
RT "Analysis of the catalytic mechanism of a fungal lipase using computer-
RT aided design and structural mutants.";
RL Protein Eng. 9:507-517(1996).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 124-392.
RX PubMed=8014587;
RA Derewenda U., Swenson L., Wei Y., Green R., Kobos P.M., Joerger R.,
RA Haas M.J., Derewenda Z.S.;
RT "Conformational lability of lipases observed in the absence of an oil-water
RT interface: crystallographic studies of enzymes from the fungi Humicola
RT lanuginosa and Rhizopus delemar.";
RL J. Lipid Res. 35:524-534(1994).
CC -!- FUNCTION: Hydrolyzes ester bonds of triglycerides as well as of their
CC derived partial glycerides with a strong 1,3-positional specificity.
CC {ECO:0000269|PubMed:11506890, ECO:0000269|PubMed:8329142}.
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:8862551, ECO:0000269|PubMed:9765593};
CC -!- ACTIVITY REGULATION: Lipase activity is maximal at a lipid-water
CC interface (interfacial activation), probably by an induced
CC conformational change that results in an increased accessibility of the
CC active site to the substrate. {ECO:0000269|PubMed:11506890}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.4 mM for triolein {ECO:0000269|PubMed:8862551};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:9765593};
CC Temperature dependence:
CC Stable up to 30 degrees Celsius. {ECO:0000269|PubMed:9765593};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:8329142}.
CC -!- MISCELLANEOUS: Limited proteolysis produces a smaller peptide starting
CC at residue Ser-124, that has altered substrate specificity and
CC biophysicochemical properties.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; M38352; AAA33878.1; -; mRNA.
DR EMBL; AF229435; AAF32408.1; -; Genomic_DNA.
DR EMBL; AY513724; AAS84458.1; -; Genomic_DNA.
DR PIR; JQ1390; JQ1390.
DR PIR; S32492; S32492.
DR PDB; 1TIC; X-ray; 2.60 A; A/B=124-392.
DR PDBsum; 1TIC; -.
DR AlphaFoldDB; P61872; -.
DR SMR; P61872; -.
DR Allergome; 7694; Rhi o Lipase.
DR ESTHER; rhidl-lipas; Lipase_3.
DR OMA; CTRCECT; -.
DR PhylomeDB; P61872; -.
DR BRENDA; 3.1.1.3; 5365.
DR SABIO-RK; P61872; -.
DR EvolutionaryTrace; P61872; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..95
FT /evidence="ECO:0000269|PubMed:11506890"
FT /id="PRO_0000017735"
FT CHAIN 96..392
FT /note="Lipase"
FT /id="PRO_0000017736"
FT REGION 50..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 268
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:8014587"
FT ACT_SITE 327
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:8014587"
FT ACT_SITE 380
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:8014587"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 152..391
FT DISULFID 163..166
FT DISULFID 358..367
FT MUTAGEN 56
FT /note="C->S: Slows folding of the peptide to the mature
FT protein."
FT /evidence="ECO:0000269|PubMed:8912667"
FT MUTAGEN 151
FT /note="Y->F: Abolishes lipase activity."
FT /evidence="ECO:0000269|PubMed:8862551"
FT MUTAGEN 206
FT /note="T->A,V: Abolishes lipase activity."
FT /evidence="ECO:0000269|PubMed:8862551"
FT MUTAGEN 206
FT /note="T->S: Reduces lipase activity by 88%. Reduces lipase
FT activity by 92%; when associated with W-212."
FT /evidence="ECO:0000269|PubMed:8862551"
FT MUTAGEN 212
FT /note="A->W: Reduces lipase activity by 44%. Reduces lipase
FT activity by 92%; when associated with S-206."
FT /evidence="ECO:0000269|PubMed:8862551"
FT MUTAGEN 215
FT /note="D->N: Reduces lipase activity by 93%."
FT /evidence="ECO:0000269|PubMed:8862551"
FT MUTAGEN 267
FT /note="H->F: Abolishes lipase activity."
FT /evidence="ECO:0000269|PubMed:8862551"
FT MUTAGEN 267
FT /note="H->S: Reduces lipase activity by 98%."
FT /evidence="ECO:0000269|PubMed:8862551"
FT MUTAGEN 327
FT /note="D->A: Abolishes lipase activity."
FT /evidence="ECO:0000269|PubMed:8862551"
FT MUTAGEN 388
FT /note="E->D: Abolishes lipase activity."
FT /evidence="ECO:0000269|PubMed:8862551"
FT CONFLICT 37
FT /note="N -> T (in Ref. 2; AAF32408)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="A -> S (in Ref. 2; AAF32408)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="N -> Y (in Ref. 2; AAF32408)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="S -> G (in Ref. 2; AAF32408 and 4; AAS84458)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="H -> N (in Ref. 2; AAF32408)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="I -> L (in Ref. 2; AAF32408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 42139 MW; D08F651EE77AA5A3 CRC64;
MVSFISISQG VSLCLLVSSM MLGSSAVPVS GKSGSSNTAV SASDNAALPP LISSRCAPPS
NKGSKSDLQA EPYNMQKNTE WYESHGGNLT SIGKRDDNLV GGMTLDLPSD APPISLSSST
NSASDGGKVV AATTAQIQEF TKYAGIAATA YCRSVVPGNK WDCVQCQKWV PDGKIITTFT
SLLSDTNGYV LRSDKQKTIY LVFRGTNSFR SAITDIVFNF SDYKPVKGAK VHAGFLSSYE
QVVNDYFPVV QEQLTAHPTY KVIVTGHSLG GAQALLAGMD LYQREPRLSP KNLSIFTVGG
PRVGNPTFAY YVESTGIPFQ RTVHKRDIVP HVPPQSFGFL HPGVESWIKS GTSNVQICTS
EIETKDCSNS IVPFTSILDH LSYFDINEGS CL
