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Sequence of PLM1_PLAFX

EC Number:3.4.23.38

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
plasmepsin I
P39898
Plasmodium falciparum (isolate HB3)
452
51461
Reaction
hydrolysis of the -Phe33-/-Leu- bond in the alpha-chain of hemoglobin, leading to denaturation of the molecule
Other sequences found for EC No. 3.4.23.38

General information:

Sequence
show sequence in fasta format
  0 MALSIKEDFS SAFAKNESAV NSSTFNNNMK TWKIQKRFQI LYVFFFLLIT GALFYYLIDN
 60 VLFPKNKKIN EIMNTSKHVI IGFSIENSHD RIMKTVKQHR LKNYIKESLK FFKTGLTQKP
120 HLGNAGDSVT LNDVANVMYY GEAQIGDNKQ KFAFIFDTGS ANLWVPSAQC NTIGCKTKNL
180 YDSNKSKTYE KDGTKVEMNY VSGTVSGFFS KDIVTIANLS FPYKFIEVTD TNGFEPAYTL
240 GQFDGIVGLG WKDLSIGSVD PVVVELKNQN KIEQAVFTFY LPFDDKHKGY LTIGGIEDRF
300 YEGQLTYEKL NHDLYWQVDL DLHFGNLTVE KATAIVDSGT SSITAPTEFL NKFFEGLDVV
360 KIPFLPLYIT TCNNPKLPTL EFRSATNVYT LEPEYYLQQI FDFGISLCMV SIIPVDLNKN
420 TFILGDPFMR KYFTVFDYDN HTVGFALAKK KL
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1100849
Francis S.E.,Gluzman I.Y.,Oksman A.,Knickerbocker A.,Mueller R.,Bryant M.L.,Sherman D.R.,Russell D.G.,Goldberg D.E.
Molecular characterization and inhibition of a Plasmodium falciparum aspartic hemoglobinase.
EMBO J.
13
306-317
1994
1100851
Goldberg D.E.,Slater A.F.G.,Beavis R.,Chait B.,Cerami A.,Henderson G.B.
Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: a catabolic pathway initiated by a specific aspartic protease.
J. Exp. Med.
173
961-969
1991
1100852
Luker K.E.,Francis S.E.,Gluzman I.Y.,Goldberg D.E.
Kinetic analysis of plasmepsins I and II aspartic proteases of the Plasmodium falciparum digestive vacuole.
Mol. Biochem. Parasitol.
79
71-78
1996
1100853
Francis S.E.,Banerjee R.,Goldberg D.E.
Biosynthesis and maturation of the malaria aspartic hemoglobinases plasmepsins I and II.
J. Biol. Chem.
272
14961-14968
1997
1100854
Banerjee R.,Liu J.,Beatty W.,Pelosof L.,Klemba M.,Goldberg D.E.
Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine.
Proc. Natl. Acad. Sci. U.S.A.
99
990-995
2002
1100855
Banerjee R.,Francis S.E.,Goldberg D.E.
Food vacuole plasmepsins are processed at a conserved site by an acidic convertase activity in Plasmodium falciparum.
Mol. Biochem. Parasitol.
129
157-165
2003
1100856
Bhaumik P.,Horimoto Y.,Xiao H.,Miura T.,Hidaka K.,Kiso Y.,Wlodawer A.,Yada R.Y.,Gustchina A.
Crystal structures of the free and inhibited forms of plasmepsin I (PMI) from Plasmodium falciparum.
J. Struct. Biol.
175
73-84
2011