LIP_THELA
ID LIP_THELA Reviewed; 291 AA.
AC O59952;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Lipase;
DE EC=3.1.1.3;
DE AltName: Full=Triacylglycerol lipase;
DE Flags: Precursor;
GN Name=LIP;
OS Thermomyces lanuginosus (Humicola lanuginosa).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Thermomyces.
OX NCBI_TaxID=5541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Boel E., Muller S., Sandal T., Kamp-Hansen P., Dalboge H.;
RT "Wild type Humicola lanuginosa cDNA encoding a lipolytic enzyme.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP MUTAGENESIS OF TRP-111.
RX PubMed=7815893; DOI=10.1007/bf02536093;
RA Holmquist M., Martinelle M., Clausen I.G., Patkar S.A., Svendsen A.,
RA Hult K.;
RT "Trp89 in the lid of Humicola lanuginosa lipase is important for efficient
RT hydrolysis of tributyrin.";
RL Lipids 29:599-603(1994).
RN [3]
RP MUTAGENESIS.
RX PubMed=7536956; DOI=10.1111/j.1365-3083.1995.tb03590.x;
RA Naver H., Lovborg U.;
RT "The importance of non-charged amino acids in antibody binding to Humicola
RT lanuginosa lipase.";
RL Scand. J. Immunol. 41:443-448(1995).
RN [4]
RP MUTAGENESIS OF GLU-109 AND TRP-111.
RX PubMed=8862552; DOI=10.1093/protein/9.6.519;
RA Martinelle M., Holmquist M., Clausen I.G., Patkar S.A., Svendsen A.,
RA Hult K.;
RT "The role of Glu87 and Trp89 in the lid of Humicola lanuginosa lipase.";
RL Protein Eng. 9:519-524(1996).
RN [5]
RP MUTAGENESIS OF SER-168.
RX PubMed=9730809; DOI=10.1021/bi972883l;
RA Peters G.H., Svendsen A., Langberg H., Vind J., Patkar S.A., Toxvaerd S.,
RA Kinnunen P.K.J.;
RT "Active serine involved in the stabilization of the active site loop in the
RT Humicola lanuginosa lipase.";
RL Biochemistry 37:12375-12383(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS), ACTIVE SITE, AND DISULFIDE BONDS.
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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 23-291, AND DISULFIDE BONDS.
RX PubMed=11106485; DOI=10.1021/bi0013905;
RA Brzozowski A.M., Savage H., Verma C.S., Turkenburg J.P., Lawson D.M.,
RA Svendsen A., Patkar S.A.;
RT "Structural origins of the interfacial activation in Thermomyces (Humicola)
RT lanuginosa lipase.";
RL Biochemistry 39:15071-15082(2000).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Active at alkaline pHs (up to pH 12 approximately).;
CC Temperature dependence:
CC Active over a broad temperature range.;
CC -!- BIOTECHNOLOGY: Used as a detergent lipase. Sold under the name Lipolase
CC by Novozymes. Engineered variants are sold under the names Lipolase
CC Ultra and LipoPrime.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AF054513; AAC08588.1; -; mRNA.
DR PDB; 1DT3; X-ray; 2.60 A; A/B=23-291.
DR PDB; 1DT5; X-ray; 2.40 A; A/B/C/D/E/F/G/H=23-291.
DR PDB; 1DTE; X-ray; 2.35 A; A/B=23-291.
DR PDB; 1DU4; X-ray; 2.50 A; A/B/C/D=23-291.
DR PDB; 1EIN; X-ray; 3.00 A; A/B/C=23-291.
DR PDB; 1GT6; X-ray; 2.20 A; A/B=23-291.
DR PDB; 1TIB; X-ray; 1.84 A; A=23-291.
DR PDB; 4DYH; X-ray; 2.00 A; A/B=23-291.
DR PDB; 4EA6; X-ray; 2.30 A; A/B=23-291.
DR PDB; 4FLF; X-ray; 2.15 A; A/B=23-291.
DR PDB; 4GBG; X-ray; 2.90 A; A/B=23-291.
DR PDB; 4GHW; X-ray; 2.60 A; A/B=23-291.
DR PDB; 4GI1; X-ray; 2.43 A; A/B=23-291.
DR PDB; 4GLB; X-ray; 2.69 A; A/B=23-291.
DR PDB; 4GWL; X-ray; 2.55 A; A/B=23-291.
DR PDB; 4KJX; X-ray; 2.10 A; A/B=23-291.
DR PDB; 4N8S; X-ray; 2.30 A; A/B=23-291.
DR PDB; 4S0X; X-ray; 2.10 A; A/B=23-291.
DR PDB; 4ZGB; X-ray; 2.30 A; A/B=23-291.
DR PDB; 5AP9; X-ray; 1.80 A; A/B=23-291.
DR PDB; 6HW1; X-ray; 2.50 A; A/B=23-291.
DR PDB; 6OR3; X-ray; 1.45 A; A=1-291.
DR PDB; 6XOK; X-ray; 1.30 A; A=1-291.
DR PDB; 6XRV; X-ray; 1.43 A; A/B/C/D/E/F=1-291.
DR PDB; 6XS3; X-ray; 2.48 A; A/B/C/D/E/F=1-291.
DR PDB; 7APN; X-ray; 2.00 A; A/B=23-291.
DR PDB; 7APP; X-ray; 1.70 A; A/B=23-291.
DR PDBsum; 1DT3; -.
DR PDBsum; 1DT5; -.
DR PDBsum; 1DTE; -.
DR PDBsum; 1DU4; -.
DR PDBsum; 1EIN; -.
DR PDBsum; 1GT6; -.
DR PDBsum; 1TIB; -.
DR PDBsum; 4DYH; -.
DR PDBsum; 4EA6; -.
DR PDBsum; 4FLF; -.
DR PDBsum; 4GBG; -.
DR PDBsum; 4GHW; -.
DR PDBsum; 4GI1; -.
DR PDBsum; 4GLB; -.
DR PDBsum; 4GWL; -.
DR PDBsum; 4KJX; -.
DR PDBsum; 4N8S; -.
DR PDBsum; 4S0X; -.
DR PDBsum; 4ZGB; -.
DR PDBsum; 5AP9; -.
DR PDBsum; 6HW1; -.
DR PDBsum; 6OR3; -.
DR PDBsum; 6XOK; -.
DR PDBsum; 6XRV; -.
DR PDBsum; 6XS3; -.
DR PDBsum; 7APN; -.
DR PDBsum; 7APP; -.
DR AlphaFoldDB; O59952; -.
DR SMR; O59952; -.
DR ChEMBL; CHEMBL2021756; -.
DR Allergome; 904; The l Lipase.
DR ESTHER; humla-1lipa; Lipase_3.
DR BRENDA; 3.1.1.3; 2711.
DR SABIO-RK; O59952; -.
DR EvolutionaryTrace; O59952; -.
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 InterPro; IPR005592; Mono/diacylglycerol_lipase_N.
DR Pfam; PF03893; Lipase3_N; 1.
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; Cleavage on pair of basic residues; Disulfide bond;
KW Hydrolase; Lipid degradation; Lipid metabolism; Signal; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..22
FT /id="PRO_0000017737"
FT CHAIN 23..291
FT /note="Lipase"
FT /id="PRO_0000017738"
FT ACT_SITE 168
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:8014587"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:8014587"
FT ACT_SITE 280
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:8014587"
FT DISULFID 44..290
FT /evidence="ECO:0000269|PubMed:8014587"
FT DISULFID 58..63
FT /evidence="ECO:0000269|PubMed:8014587"
FT DISULFID 126..129
FT /evidence="ECO:0000269|PubMed:8014587"
FT MUTAGEN 109
FT /note="E->A: 35-70% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:8862552"
FT MUTAGEN 111
FT /note="W->E,F,G,L: Altered chain length specificity."
FT /evidence="ECO:0000269|PubMed:7815893,
FT ECO:0000269|PubMed:8862552"
FT MUTAGEN 168
FT /note="S->A: Decrease in liposome binding."
FT /evidence="ECO:0000269|PubMed:9730809"
FT HELIX 26..41
FT /evidence="ECO:0007829|PDB:6XOK"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6XOK"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:4GLB"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1TIB"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:6XOK"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:6XOK"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:6XOK"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:6XOK"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:6XOK"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:6XOK"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:6XOK"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6XOK"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:6XOK"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6XOK"
FT HELIX 133..156
FT /evidence="ECO:0007829|PDB:6XOK"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:6XOK"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:6XOK"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6XOK"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:6XOK"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:6XOK"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:6OR3"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:6XOK"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:6XOK"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:6XOK"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:6XOK"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:6XOK"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:6XOK"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6XRV"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:7APP"
FT HELIX 277..281
FT /evidence="ECO:0007829|PDB:6XOK"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:6XOK"
SQ SEQUENCE 291 AA; 31807 MW; 170ACEDF791DB07B CRC64;
MRSSLVLFFV SAWTALASPI RREVSQDLFN QFNLFAQYSA AAYCGKNNDA PAGTNITCTG
NACPEVEKAD ATFLYSFEDS GVGDVTGFLA LDNTNKLIVL SFRGSRSIEN WIGNLNFDLK
EINDICSGCR GHDGFTSSWR SVADTLRQKV EDAVREHPDY RVVFTGHSLG GALATVAGAD
LRGNGYDIDV FSYGAPRVGN RAFAEFLTVQ TGGTLYRITH TNDIVPRLPP REFGYSHSSP
EYWIKSGTLV PVTRNDIVKI EGIDATGGNN QPNIPDIPAH LWYFGLIGTC L
