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Contributes toGO:0008745N-acetylmuramoyl-L-alanine amidase activityPMID:16103125IDA: Inferred from Direct Assay F
This annotation made on page: BACAN:Q81WA9
By: Strandquistg (group Team DirtyChubi) on 2016-04-06 12:23:13 CDT.



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Entry TypeChallenging User,GroupTime/DateChallenge ReasonPoints/Assessment
ChallengeMnguy1,
Team Blue B
2016-04-18 11:33:42 CDT

Base on your explanation in your note portion, you didn't clarify why this gene had N-acetylmuramoyl-L_alanine amides activity. You could have your go term as more general such as lytic activity. As for protein to act as N-acetylmuramoyl-L alanine amidase activity, it mainly lysed at N-terminal domain of PlyL to give rise to 2,4 dinitrophenyl- alanine which was absorbed in Figure 4A (full length gene) and 4B (N terminal domain of the gene). Compared the rate of absorbance of the compound, it was higher at N terminal compared to full length protein.

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Suzialeksander2016-06-27 12:57:10 CDTYou need to be an instructor to view these notes.Updated by Instructor
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Suzialeksander2016-05-20 16:32:32 CDTYou need to be an instructor to view these notes.Requires Changes
Protein
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Go term
Evidence
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Notes
Unique/Original
Public
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AAJohnson2016-05-03 15:19:25 CDTNo notes given.Acceptable
Protein
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Go term
Evidence
With/From
Notes
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DanielRenfro2016-04-23 11:44:33 CDT

This annotation has been flagged because it has been edited since last assessment

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
Contributes to GO:0008745 N-acetylmuramoyl-L-alanine amidase activity PMID:16103125 IDA: Inferred from Direct Assay F PlyL is an endolysin enzyme with 2 separate domains, an N-terminal catalytic domain, and a C-terminal cell wall binding domain. This annotation is for the N-terminal domain of PlyL.

Peptidoglycan from B. subtilis was subjected to both the full-length PlyL and the N-terminal domain only. In supplemental figure 1, (see link: http://www.jbc.org/content/suppl/2005/08/16/M502723200.DC1/Suppdata.pdf) the amount of 2,4-dinitrophenyl-alanine is shown to increase sharply, indicating that PlyL is an N-acetylmuramoyl-L-alanine amidase. Additionally, the figure shows that alanine is increased even more when the N-terminal domain alone is used, compared to the full-length protein.

As additional support that PlyL is an amidase, figure 2 compares the crystal structure of PlyL to other known amidase enzymes.

Figure 4 shows a time course assay where the purified endolysin (PlyL) was able to lyse 4 different bacillus species cultures within 400 seconds. In 4a, the lysing capabilities of the full-length version of PlyL are shown. In 4b, the lysing capabilities of the N-terminal portion only are shown. The N-terminal domain by itself is more effective at cleaving Bacillus species than the entirety of PlyL. ||complete
CACAO 11527

on BACAN:Q81WA9
Flagged