Extracellular methionine amino peptidase (MAP) production by Streptomyces gedanensis in solid-state fermentation

Rahulan, Raji; Manjunath, G. M.; Nampoothiri, K. Madhavan; Pandey, Ashok

doi:10.1590/s1516-89132014000200005

Cited by 2 publications

(1 citation statement)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Aminopeptidases can be categorized on the basis of their substrate specificity (broad or narrow), catalytic mechanism (serine, metallo, cysteine peptidases), cellular location (cytosolic, membrane, and microsomal), and molecular structure [5][6][7][8][9]. Examples of these enzymes are methionine aminopeptidase, arginine aminopeptidase, leucine aminopeptidase, aminopeptidase A, and aminopeptidase P [10][11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Structure-Function and Industrial Relevance of Bacterial Aminopeptidase P

et al. 2021

View full text Add to dashboard Cite

Aminopeptidase P (APPro, E.C 3.4.11.9) cleaves N-terminal amino acids from peptides and proteins where the penultimate residue is proline. This metal-ion-dependent enzyme shares a similar fold, catalytic mechanism, and substrate specificity with methionine aminopeptidase and prolidase. It adopts a canonical pita bread fold that serves as a structural basis for the metal-dependent catalysis and assembles as a tetramer in crystals. Similar to other metalloaminopeptidase, APPro requires metal ions for its maximal enzymatic activity, with manganese being the most preferred cation. Microbial aminopeptidase possesses unique characteristics compared with aminopeptidase from other sources, making it a great industrial enzyme for various applications. This review provides a summary of recent progress in the study of the structure and function of aminopeptidase P and describes its various applications in different industries as well as its significance in the environment.

show abstract