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Q10740

- LKHA4_YEAST

UniProt

Q10740 - LKHA4_YEAST

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Protein

Leukotriene A-4 hydrolase homolog

Gene

LAP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Aminopeptidase that preferentially cleaves tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze an epoxide moiety of LTA4 to form LTB4 (in vitro).5 Publications

Catalytic activityi

(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Enzyme regulationi

Inhibited 3-(4-benzyloxyphenyl)-2-(R)-amino-1-propanethiol (thioamine) and N-hydroxy-N-(2-(S)-amino-3-(4-benzyloxyphenyl)propyl)-5-carboxypen-tanamide (hydroxamic acid). The aminopeptidase activity is stimulated by LTA4.2 Publications

Kineticsi

  1. KM=1.5 mM for Leu-p-nitroanilide3 Publications
  2. KM=1.8 mM for Met-p-nitroanilide3 Publications
  3. KM=2.0 mM for Ala-p-nitroanilide3 Publications

Vmax=520 nmol/min/mg enzyme with Leu-p-nitroanilide as substrate3 Publications

Vmax=360 nmol/min/mg enzyme with Met-p-nitroanilide as substrate3 Publications

Vmax=170 nmol/min/mg enzyme with Ala-p-nitroanilide as substrate3 Publications

pH dependencei

Optimum pH is about 7.3.3 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi340 – 3401Zinc; catalytic
Active sitei341 – 3411Proton acceptor
Metal bindingi344 – 3441Zinc; catalytic
Metal bindingi363 – 3631Zinc; catalytic
Active sitei429 – 4291Proton donor

GO - Molecular functioni

  1. aminopeptidase activity Source: SGD
  2. epoxide hydrolase activity Source: SGD
  3. leukotriene-A4 hydrolase activity Source: SGD
  4. metallopeptidase activity Source: UniProtKB-KW
  5. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cellular lipid metabolic process Source: SGD
  2. leukotriene biosynthetic process Source: UniProtKB-KW
  3. peptide catabolic process Source: UniProtKB
  4. protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Leukotriene biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YNL045W-MONOMER.
ReactomeiREACT_189270. Synthesis of Leukotrienes (LT) and Eoxins (EX).
UniPathwayiUPA00878.

Protein family/group databases

MEROPSiM01.034.

Names & Taxonomyi

Protein namesi
Recommended name:
Leukotriene A-4 hydrolase homolog (EC:3.3.2.6)
Short name:
LTA-4 hydrolase
Alternative name(s):
Leucine aminopeptidase 2
Leukotriene A(4) hydrolase
Gene namesi
Name:LAP2
Ordered Locus Names:YNL045W
ORF Names:N2535
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIV

Organism-specific databases

CYGDiYNL045w.
SGDiS000004990. LAP2.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi244 – 2441Y → F: Reduces strongly the substrate affinity. 1 Publication
Mutagenesisi316 – 3161E → A, Q or D: Abolishes the aminopeptidase activity. 1 Publication
Mutagenesisi340 – 3401H → Q: Abolishes the epoxide hydrolase and aminopeptidase activities. 1 Publication
Mutagenesisi341 – 3411E → Q: Abolishes aminopeptidase activity. No effect on the epoxide hydrolase activity. 1 Publication
Mutagenesisi344 – 3441H → Q: Abolishes the epoxide hydrolase and aminopeptidase activities. 1 Publication
Mutagenesisi363 – 3631E → Q: Abolishes the epoxide hydrolase activity. 1 Publication
Mutagenesisi424 – 4241F → Y: Increases the aminopeptidase activity and decreases the epoxide hydrolase activity. 1 Publication
Mutagenesisi429 – 4291Y → F: Abolishes the aminopeptidase activity and decreases the epoxide hydrolase activity. 1 Publication
Mutagenesisi627 – 6271R → K or A: Abolishes the aminopeptidase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 671671Leukotriene A-4 hydrolase homologPRO_0000095129Add
BLAST

Proteomic databases

MaxQBiQ10740.
PaxDbiQ10740.
PeptideAtlasiQ10740.

Expressioni

Gene expression databases

GenevestigatoriQ10740.

Interactioni

Protein-protein interaction databases

BioGridi35779. 26 interactions.
DIPiDIP-4371N.
IntActiQ10740. 6 interactions.
MINTiMINT-542331.
STRINGi4932.YNL045W.

Structurei

Secondary structure

1
671
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 486Combined sources
Beta strandi51 – 544Combined sources
Helixi64 – 663Combined sources
Beta strandi67 – 7913Combined sources
Turni80 – 834Combined sources
Beta strandi84 – 9512Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi105 – 1095Combined sources
Beta strandi111 – 12010Combined sources
Beta strandi127 – 1293Combined sources
Turni134 – 1363Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi147 – 15913Combined sources
Beta strandi164 – 1696Combined sources
Turni171 – 1733Combined sources
Beta strandi175 – 1784Combined sources
Beta strandi180 – 1834Combined sources
Turni186 – 1894Combined sources
Helixi190 – 1923Combined sources
Beta strandi204 – 2118Combined sources
Beta strandi216 – 2227Combined sources
Beta strandi232 – 24110Combined sources
Helixi243 – 2453Combined sources
Beta strandi248 – 2525Combined sources
Beta strandi254 – 2596Combined sources
Beta strandi262 – 2665Combined sources
Helixi268 – 27811Combined sources
Turni279 – 2813Combined sources
Helixi282 – 29211Combined sources
Beta strandi297 – 2993Combined sources
Beta strandi303 – 3053Combined sources
Beta strandi312 – 3154Combined sources
Beta strandi321 – 3233Combined sources
Helixi325 – 3273Combined sources
Beta strandi330 – 3323Combined sources
Helixi336 – 3449Combined sources
Turni348 – 3503Combined sources
Beta strandi351 – 3555Combined sources
Helixi356 – 3594Combined sources
Helixi360 – 37819Combined sources
Helixi380 – 39920Combined sources
Beta strandi401 – 4033Combined sources
Helixi404 – 4074Combined sources
Beta strandi409 – 4113Combined sources
Beta strandi416 – 4183Combined sources
Helixi420 – 4234Combined sources
Helixi427 – 44216Combined sources
Helixi446 – 45914Combined sources
Turni460 – 4623Combined sources
Beta strandi463 – 4653Combined sources
Helixi467 – 47711Combined sources
Helixi479 – 4813Combined sources
Helixi482 – 4865Combined sources
Helixi490 – 4956Combined sources
Helixi508 – 52316Combined sources
Turni524 – 5263Combined sources
Helixi530 – 5367Combined sources
Helixi539 – 5424Combined sources
Helixi547 – 55812Combined sources
Beta strandi562 – 5654Combined sources
Helixi572 – 5743Combined sources
Helixi576 – 58510Combined sources
Helixi587 – 5915Combined sources
Helixi596 – 60813Combined sources
Helixi612 – 6143Combined sources
Helixi615 – 6217Combined sources
Turni622 – 6243Combined sources
Helixi628 – 63912Combined sources
Helixi643 – 65311Combined sources
Helixi654 – 6563Combined sources
Helixi659 – 66810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XPYX-ray2.73A40-671[»]
2XPZX-ray2.30A40-671[»]
2XQ0X-ray1.96A40-669[»]
ProteinModelPortaliQ10740.
SMRiQ10740. Positions 40-671.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ10740.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 1863Substrate binding
Regioni311 – 3166Substrate binding

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

eggNOGiCOG0308.
GeneTreeiENSGT00530000063003.
HOGENOMiHOG000293296.
InParanoidiQ10740.
KOiK01254.
OMAiSPASVCQ.
OrthoDBiEOG7DFXMZ.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR012777. Leukotriene_A4_hydrolase.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
SUPFAMiSSF48371. SSF48371. 1 hit.
TIGRFAMsiTIGR02411. leuko_A4_hydro. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10740-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFLLPFVIRH SSSIYLPTLR FRGLLTVISR NIHISTPHKM LPLSIEQRRP
60 70 80 90 100
SRSPEYDQST LSNYKDFAVL HTDLNLSVSF EKSAISGSVT FQLKKLHEGK
110 120 130 140 150
NKSDELHLDT SYLDVQEVHI DGSKADFQIE QRKEPLGSRL VINNASCNDN
160 170 180 190 200
FTLNIQFRTT DKCTALQWLN SKQTKGGKPY VFSQLEAIHA RSLFPCFDTP
210 220 230 240 250
SVKSTFTASI ESPLPVVFSG IRIEDTSKDT NIYRFEQKVP IPAYLIGIAS
260 270 280 290 300
GDLSSAPIGP RSTVYTEPFR LKDCQWEFEN DVEKFIQTAE KIIFEYEWGT
310 320 330 340 350
YDILVNVDSY PYGGMESPNM TFATPTLIAH DRSNIDVIAH ELAHSWSGNL
360 370 380 390 400
VTNCSWNHFW LNEGWTVYLE RRIIGAIHGE PTRHFSALIG WSDLQNSIDS
410 420 430 440 450
MKDPERFSTL VQNLNDNTDP DDAFSTVPYE KGFNLLFHLE TILGGKAEFD
460 470 480 490 500
PFIRHYFKKF AKKSLDTFQF LDTLYEFYPE KKEILDSVDW ETWLYKPGMP
510 520 530 540 550
PRPHFITALA DNVYQLADKW VEMAQHLKTT EDFRSEFNAI DIKDFNSNQL
560 570 580 590 600
VLFLETLTQN GHSNKKPKDF DWAKFPVASR ALLDIYQDNI VKSQNAEVVF
610 620 630 640 650
KMFKFQIFAK LQEEYKHLAD WLGTVGRMKF VRPGYRLLNS VDRRLALATF
660 670
DKFKDTYHPI CKALVKQDLG L
Length:671
Mass (Da):77,353
Last modified:October 1, 1996 - v1
Checksum:i454E40F030BF28FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94547 Genomic DNA. Translation: CAA64237.1.
Z71321 Genomic DNA. Translation: CAA95912.1.
BK006947 Genomic DNA. Translation: DAA10500.1.
PIRiS61099.
RefSeqiNP_014353.1. NM_001182884.1.

Genome annotation databases

EnsemblFungiiYNL045W; YNL045W; YNL045W.
GeneIDi855682.
KEGGisce:YNL045W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94547 Genomic DNA. Translation: CAA64237.1 .
Z71321 Genomic DNA. Translation: CAA95912.1 .
BK006947 Genomic DNA. Translation: DAA10500.1 .
PIRi S61099.
RefSeqi NP_014353.1. NM_001182884.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XPY X-ray 2.73 A 40-671 [» ]
2XPZ X-ray 2.30 A 40-671 [» ]
2XQ0 X-ray 1.96 A 40-669 [» ]
ProteinModelPortali Q10740.
SMRi Q10740. Positions 40-671.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35779. 26 interactions.
DIPi DIP-4371N.
IntActi Q10740. 6 interactions.
MINTi MINT-542331.
STRINGi 4932.YNL045W.

Protein family/group databases

MEROPSi M01.034.

Proteomic databases

MaxQBi Q10740.
PaxDbi Q10740.
PeptideAtlasi Q10740.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YNL045W ; YNL045W ; YNL045W .
GeneIDi 855682.
KEGGi sce:YNL045W.

Organism-specific databases

CYGDi YNL045w.
SGDi S000004990. LAP2.

Phylogenomic databases

eggNOGi COG0308.
GeneTreei ENSGT00530000063003.
HOGENOMi HOG000293296.
InParanoidi Q10740.
KOi K01254.
OMAi SPASVCQ.
OrthoDBi EOG7DFXMZ.

Enzyme and pathway databases

UniPathwayi UPA00878 .
BioCyci YEAST:YNL045W-MONOMER.
Reactomei REACT_189270. Synthesis of Leukotrienes (LT) and Eoxins (EX).

Miscellaneous databases

EvolutionaryTracei Q10740.
NextBioi 979984.
PROi Q10740.

Gene expression databases

Genevestigatori Q10740.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR012777. Leukotriene_A4_hydrolase.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view ]
PANTHERi PTHR11533. PTHR11533. 1 hit.
Pfami PF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view ]
PRINTSi PR00756. ALADIPTASE.
SUPFAMi SSF48371. SSF48371. 1 hit.
TIGRFAMsi TIGR02411. leuko_A4_hydro. 1 hit.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of 12.8 kb from the left arm of chromosome XIV reveals a sigma element, a pro-tRNA and six complete open reading frames, one of which encodes a protein similar to the human leukotriene A4 hydrolase."
    Nasr F., Becam A.-M., Herbert C.J.
    Yeast 12:493-499(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Cloning and characterization of a bifunctional leukotriene A(4) hydrolase from Saccharomyces cerevisiae."
    Kull F., Ohlson E., Haeggstroem J.Z.
    J. Biol. Chem. 274:34683-34690(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  5. "Saccharomyces cerevisiae leukotriene A4 hydrolase: formation of leukotriene B4 and identification of catalytic residues."
    Kull F., Ohlson E., Lind B., Haeggstroem J.Z.
    Biochemistry 40:12695-12703(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-340; GLU-341; HIS-344; GLU-363; PHE-424 AND TYR-429.
  6. "Crystallization and X-ray diffraction data analysis of leukotriene A4 hydrolase from Saccharomyces cerevisiae."
    Andersson B., Kull F., Haeggstroem J.Z., Thunnissen M.M.G.M.
    Acta Crystallogr. D 59:1093-1095(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Leukotriene A4 hydrolase, insights into the molecular evolution by homology modeling and mutational analysis of enzyme from Saccharomyces cerevisiae."
    Tholander F., Kull F., Ohlson E., Shafqat J., Thunnissen M.M.G.M., Haeggstroem J.Z.
    J. Biol. Chem. 280:33477-33486(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS.
  10. "A conserved tyrosine residue of Saccharomyces cerevisiae leukotriene A4 hydrolase stabilizes the transition state of the peptidase activity."
    Thompson M.W., Archer E.D., Romer C.E., Seipelt R.L.
    Peptides 27:1701-1709(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-244.
  11. "A leukotriene A4 hydrolase-related aminopeptidase from yeast undergoes induced fit upon inhibitor binding."
    Helgstrand C., Hasan M., Uysal H., Haeggstrom J.Z., Thunnissen M.M.
    J. Mol. Biol. 406:120-134(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 40-669 IN COMPLEX WITH ZINC IONS AND BESTATIN, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.

Entry informationi

Entry nameiLKHA4_YEAST
AccessioniPrimary (citable) accession number: Q10740
Secondary accession number(s): D6W1D4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5590 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families
  5. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  6. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3