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adenylation
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adenylation
adenylation, n. Biochem. (əˌdɛnɪˈleɪʃən) [f. adenyl n. + -ation.] The covalent attachment of an adenylate moiety to a molecule.1967 Biochem. & Biophysical Res. Communications XXVIII. 740 The interconversion of the two forms of glutamine synthetase is an ‘adenylation’ of glutamine synthetase by ATP. ...
Oxford English Dictionary
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Didemnin
On DidB, the adenylation (A) domain is loaded by pyruvate and subsequently reduced in its cis conformation by the ketoreductase (KR) domain, yielding the The adenylation (A) domain of didD is loaded with leucine and subsequently N-methylated by the methyltransferase (MT) domain and converted into N-methylated
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adenylating
adenylating, vbl. n. and ppl. a. Biochem. (əˈdɛnɪleɪtɪŋ) [Back-formation from *adenylation n.: see -ing2, -ing1.] A. ppl. a. That causes the introduction of an adenyl moiety into a molecule.1969 FEBS Lett. III. 263 (heading) Independent genetic regulation of glutamine synthetase and its inactivating...
Oxford English Dictionary
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Atromentin
code for biosynthesis
The nonribosomal peptide synthetase-like enzyme (atromentin synthetase) that symmetrically condenses two monomers of 4-HPP has an adenylation The adenylation domain of this NRPS-like enzyme accepts 4-HPP as determined by the ATP-PPi-exchange assay.
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adenylylation
adenylylation, n. Biochem. (əˌdɛnɪlaɪˈleɪʃən) [f. adenylic a. + -yl + -ation.] = *adenylation n.1967 Proc. Nat. Acad. Sci. LVIII. 648 The physiological significance of the adenylylation mechanism. 1969 Federation Proc. XXVIII. 467/2 (title) Enzymatic adenylylation of pyrophosphate by 3{p},5{p} cycli...
Oxford English Dictionary
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Cereulide
CesA1 adds ketoisocaproic acid to the adenylation domain. In module CesA2, L-alanine is added to the adenylation domain.
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Xenortide
The first NRPS (XndA) consists of a condensation, adenylation, methylation, and thiolation domain, and has been implicated for the loading of N-methylleucine The second NRPS (XndB) consists of a condensation, adenylation, methylation, thiolation, and terminal condensation domains.
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Codons at for transcription vs translation Why are start and stop codons present at translation level but not at transcription level? And how will I obtain a protein at transcription level? Thanks in advance
The equivalent 'start' and 'stop' signs for transcription are promoters) and poly-adenylation-sites (at least for eukaryotic mRNA). transcription:
* transcription factors bind the promoters on the DNA and recruit RNA polymerase to that site so that transcription can start
* poly-adenylation-site
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UBA1
and Ub; second, the catalytic cysteine half-domains, which contain the E1 active site cysteine inserted into each of the adenylation domains; third, a Specifically, UBA1 catalyzes the ATP-dependent adenylation of ubiquitin, thereby forming a thioester bond between the two.
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Villin 1
Two mRNAs of 2.7 kb and 3.5 kb have been observed; they result from utilization of alternate poly-adenylation signals present in the terminal exon.
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Ornibactin
The domains are as follows: adenylation (A), peptidyl carrier (P), condensation (C), and epimerase (E).
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Psymberin
KR, ketoreductase; KS0, non-elongating ketoreductase; OMT, O-methyltranfserase; C, nonribosomal peptide synthetase (NRPS) condensation domain; A, NRPS adenylation
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Andrimid
Biosynthesis
Abbreviations: ketosynthase (KS), chain length factor (CLF), dehydrogenase (DH), ketoreductase (KR), thiolation (T), transglutaminase (TG), adenylation Additional characteristics of the Andrimid assembly line are the beginning enzymes such as AdmH containing the aminomutase, AdmJ containing the β-Phe adenylation
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Sulfur carrier protein ThiS adenylyltransferase
The enzyme catalyses the adenylation of ThiS, a sulfur carrier protein involved in the biosynthesis of thiamine.
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Flavin adenine dinucleotide synthetase 1
Function
This gene encodes the enzyme that catalyzes adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.
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