3.4.11.19: D-stereospecific aminopeptidase
This is an abbreviated version!
For detailed information about D-stereospecific aminopeptidase, go to the full flat file.
Word Map on EC 3.4.11.19
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3.4.11.19
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ochrobactrum
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anthropi
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beta-lactamases
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penicillin-binding
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penicillin-recognizing
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aminopeptidases
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point-group
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d,d-carboxypeptidase
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non-sporulating
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synthesis
- 3.4.11.19
- ochrobactrum
- anthropi
- beta-lactamases
-
penicillin-binding
-
penicillin-recognizing
- aminopeptidases
-
point-group
- d,d-carboxypeptidase
-
non-sporulating
- synthesis
Reaction
Release of an N-terminal D-amino acid from a peptide, Xaa-/-Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-Amino acid amides and methyl esters also are hydrolysed, as is glycine amide =
Synonyms
D-aminopeptidase, DAP, GdaA, glycine D-alanine aminopeptidase
ECTree
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General Information
General Information on EC 3.4.11.19 - D-stereospecific aminopeptidase
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physiological function
no significant differences are observed in the vegetative growth and conidiation on minimal and complete media in the enzyme gene disruptant or overexpression strains
physiological function
GdaA is largely responsible for intracellular glycine and D-alanine aminopeptidase activities in Aspergillus oryzae during stationary-phase growth in liquid media. In addition, the activity increases in response to the depletion of nitrogen or carbon sources in the growth media. No significant differences are observed in the vegetative growth and conidiation on minimal and complete media in the GdaA deletion or overexpression strains, and control strains