Dipeptidyl aminopeptidase IV from Stenotrophomonas maltophilia exhibits activity against a substrate containing a 4-hydroxyproline residue

Journal of Bacteriology

Volumn 190, Issue 23, 2008, Pages 7819-7829

  Nakajima, Yoshitaka ^a   Ito, Kiyoshi ^a   Toshima, Tsubasa ^a   Egawa, Takashi ^a   Zheng, Heng ^a,c   Oyama, Hiroshi ^a,d   Wu, Yu Fan ^a   Takahashi, Eiji ^b   Kyono, Kiyoshi ^b   Yoshimoto, Tadashi ^a  

^a NAGASAKI UNIVERSITY   (Japan)

^b MITSUBISHI TANABE PHARMA CORPORATION   (Japan)

^c CHINA PHARMACEUTICAL UNIVERSITY   (China)

^d NIHON PHARMACEUTICAL UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

DIPEPTIDYL PEPTIDASE IV; HYDROXYPROLINE; PLATINUM; PROLINE; SELENOMETHIONINE;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS; STENOTROPHOMONAS MALTOPHILIA;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; DIPEPTIDYL PEPTIDASES; HYDROXYPROLINE; MODELS, MOLECULAR; OPEN READING FRAMES; STENOTROPHOMONAS MALTOPHILIA; SUBSTRATE SPECIFICITY;

MAMMALIA; STENOTROPHOMONAS; STENOTROPHOMONAS MALTOPHILIA; SUS;

EID: 57349169308     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.02010-07     Document Type: Article

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