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Lipase (EC 3.1.1.3) (RDL) (Triacylglycerol lipase) (ROL)

 LIP_RHIOR               Reviewed;         392 AA.
P61872; P21811; Q12237; Q5J329; Q9P312;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 1.
23-MAY-2018, entry version 73.
RecName: Full=Lipase;
EC=3.1.1.3;
AltName: Full=RDL;
AltName: Full=Triacylglycerol lipase;
Short=ROL;
Flags: Precursor;
Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
NCBI_TaxID=64495;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ATCC 34612;
PubMed=1756969; DOI=10.1016/0378-1119(91)90594-2;
Haas M.J., Berka T.R.;
"Cloning, expression and characterization of a cDNA encoding a lipase
from Rhizopus delemar.";
Gene 109:107-113(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 124-128.
STRAIN=DSM 853 / CBS 327.47;
PubMed=9765593; DOI=10.1016/S0167-4781(98)00104-3;
Beer H.D., McCarthy J.E.G., Bornscheuer U.T., Schmid R.D.;
"Cloning, expression, characterization and role of the leader sequence
of a lipase from Rhizopus oryzae.";
Biochim. Biophys. Acta 1399:173-180(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 96-392, AND PROTEIN SEQUENCE OF
124-144.
PubMed=15710378; DOI=10.1016/j.febslet.2004.12.068;
Sayari A., Frikha F., Miled N., Mtibaa H., Ben-Ali Y., Verger R.,
Gargouri Y.;
"N-terminal peptide of Rhizopus oryzae lipase is important for its
catalytic properties.";
FEBS Lett. 579:976-982(2005).
[4]
PROTEIN SEQUENCE OF 96-115, FUNCTION, AND ENZYME REGULATION.
PubMed=11506890; DOI=10.1016/S0300-9084(01)01283-4;
Ben-Salah A., Sayari A., Verger R., Gargouri Y.;
"Kinetic studies of Rhizopus oryzae lipase using monomolecular film
technique.";
Biochimie 83:463-469(2001).
[5]
MUTAGENESIS OF CYS-56.
PubMed=8912667; DOI=10.1042/bj3190351;
Beer H.D., Wohlfahrt G., Schmid R.D., McCarthy J.E.G.;
"The folding and activity of the extracellular lipase of Rhizopus
oryzae are modulated by a prosequence.";
Biochem. J. 319:351-359(1996).
[6]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TYR-151; THR-206;
ALA-212; ASP-215; HIS-267; ASP-327 AND GLU-388.
PubMed=8862551; DOI=10.1093/protein/9.6.507;
Beer H.D., Wohlfahrt G., McCarthy J.E.G., Schomburg D., Schmid R.D.;
"Analysis of the catalytic mechanism of a fungal lipase using
computer-aided design and structural mutants.";
Protein Eng. 9:507-517(1996).
[7]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 124-392.
PubMed=8014587;
Derewenda U., Swenson L., Wei Y., Green R., Kobos P.M., Joerger R.,
Haas M.J., Derewenda Z.S.;
"Conformational lability of lipases observed in the absence of an oil-
water interface: crystallographic studies of enzymes from the fungi
Humicola lanuginosa and Rhizopus delemar.";
J. Lipid Res. 35:524-534(1994).
-!- FUNCTION: Hydrolyzes ester bonds of triglycerides as well as of
their derived partial glycerides with a strong 1,3-positional
specificity. {ECO:0000269|PubMed:11506890}.
-!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
carboxylate.
-!- ENZYME REGULATION: Lipase activity is maximal at a lipid-water
interface (interfacial activation), probably by an induced
conformational change that results in an increased accessibility
of the active site to the substrate.
{ECO:0000269|PubMed:11506890}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=4.4 mM for triolein {ECO:0000269|PubMed:8862551};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- MISCELLANEOUS: Limited proteolysis produces a smaller peptide
starting at residue Ser-124, that has altered substrate
specificity and biophysicochemical properties.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M38352; AAA33878.1; -; mRNA.
EMBL; AF229435; AAF32408.1; -; Genomic_DNA.
EMBL; AY513724; AAS84458.1; -; Genomic_DNA.
PIR; JQ1390; JQ1390.
PDB; 1TIC; X-ray; 2.60 A; A/B=124-392.
PDBsum; 1TIC; -.
ProteinModelPortal; P61872; -.
SMR; P61872; -.
Allergome; 7694; Rhi o Lipase.
ESTHER; rhidl-lipas; Lipase_3.
OMA; TVIQQPS; -.
PhylomeDB; P61872; -.
BRENDA; 3.1.1.3; 5365.
EvolutionaryTrace; P61872; -.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR002921; Fungal_lipase-like.
Pfam; PF01764; Lipase_3; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00120; LIPASE_SER; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cleavage on pair of basic residues;
Direct protein sequencing; Disulfide bond; Hydrolase;
Lipid degradation; Lipid metabolism; Metal-binding; Secreted; Signal.
SIGNAL 1 26 {ECO:0000255}.
PROPEP 27 95 {ECO:0000269|PubMed:11506890}.
/FTId=PRO_0000017735.
CHAIN 96 392 Lipase.
/FTId=PRO_0000017736.
ACT_SITE 268 268 Nucleophile.
{ECO:0000305|PubMed:8014587}.
ACT_SITE 327 327 Charge relay system.
{ECO:0000269|PubMed:8014587}.
ACT_SITE 380 380 Charge relay system.
{ECO:0000305|PubMed:8014587}.
METAL 379 379 Calcium. {ECO:0000250}.
DISULFID 152 391
DISULFID 163 166
DISULFID 358 367
MUTAGEN 56 56 C->S: Slows folding of the peptide to the
mature protein.
{ECO:0000269|PubMed:8912667}.
MUTAGEN 151 151 Y->F: Abolishes lipase activity.
{ECO:0000269|PubMed:8862551}.
MUTAGEN 206 206 T->A,V: Abolishes lipase activity.
{ECO:0000269|PubMed:8862551}.
MUTAGEN 206 206 T->S: Reduces lipase activity by 88%.
Reduces lipase activity by 92%; when
associated with W-212.
{ECO:0000269|PubMed:8862551}.
MUTAGEN 212 212 A->W: Reduces lipase activity by 44%.
Reduces lipase activity by 92%; when
associated with S-206.
{ECO:0000269|PubMed:8862551}.
MUTAGEN 215 215 D->N: Reduces lipase activity by 93%.
{ECO:0000269|PubMed:8862551}.
MUTAGEN 267 267 H->F: Abolishes lipase activity.
{ECO:0000269|PubMed:8862551}.
MUTAGEN 267 267 H->S: Reduces lipase activity by 98%.
{ECO:0000269|PubMed:8862551}.
MUTAGEN 327 327 D->A: Abolishes lipase activity.
{ECO:0000269|PubMed:8862551}.
MUTAGEN 388 388 E->D: Abolishes lipase activity.
{ECO:0000269|PubMed:8862551}.
CONFLICT 37 37 N -> T (in Ref. 2; AAF32408).
{ECO:0000305}.
CONFLICT 46 46 A -> S (in Ref. 2; AAF32408).
{ECO:0000305}.
CONFLICT 74 74 N -> Y (in Ref. 2; AAF32408).
{ECO:0000305}.
CONFLICT 118 118 S -> G (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 257 257 H -> N (in Ref. 2; AAF32408).
{ECO:0000305}.
CONFLICT 377 377 I -> L (in Ref. 2; AAF32408).
{ECO:0000305}.
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


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