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O-acetylhomoserine thiol-lyase

O-acetylhomoserine (thiol)-lyase

(Science: enzyme) With hydrogen sulfide, forms homocysteine

registry number: EC 4.2.99.10

Synonym: acetylhomoserine sulfhydrylase, homocysteine synthase, oah sulfhydrylase, o-acetylhomoserine sulfhydrylase, o-acetyl-l-homoserine sulfhydrylase, o-acetylhomoserine-o-acetylserine sulfhydrylase, met25 sulfhydrylase, o-acetylserine-o-acetylhomoserine sulfohydro-lyase, aahshase


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Re: How to prove that thiol groups are de-protected?

MALDI-TOF mass spec comes to mind to check if the disulfide is broken. I suppose it depends what instruments are at hand.

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by jonmoulton
Wed May 02, 2012 10:10 pm
 
Forum: Molecular Biology
Topic: How to prove that thiol groups are de-protected?
Replies: 2
Views: 692

How to prove that thiol groups are de-protected?

... I'm trying to link chemically a protein with a DNA oligonucleotide. I think one of the simplest way would be to use Michael addition, where thiol group reacts with C=C electron deficient bond. Befor trying to work with proteins, which could be hard, I'm trying to ligate two DNA oligonucleotides, ...

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by sergii
Wed May 02, 2012 7:32 pm
 
Forum: Molecular Biology
Topic: How to prove that thiol groups are de-protected?
Replies: 2
Views: 692

Re: how to memorize the amino acid

... an exception. Proline as well, since it is an imino acid. Alanine is the "basic" amino acid. Now, serine and cysteine are hydroxy- and thiol derivatives. Valine and leucine are dimethyl and isopropyl derivatives. Isoleucine is not iso- for no reason, so you move the methyl by one carbon. ...

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by JackBean
Thu Feb 09, 2012 9:52 am
 
Forum: General Discussion
Topic: how to memorize the amino acid
Replies: 4
Views: 2116

Denaturation and refolding of an enzyme

... answering the question? Q2.What is the function of cysteine in the renaturation reaction? I think the answer : The side chain on cysteine is thiol participates in enzymatic reactions and act as nucleophile. Cysteine residues play a valuable role by crosslinking proteins, which increases the ...

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by enzsel
Thu Dec 02, 2010 1:54 pm
 
Forum: Cell Biology
Topic: Denaturation and refolding of an enzyme
Replies: 3
Views: 2356

Protein bonding(antigens)

... Tertiary structure is largely maintained by disulfide bonds. Disulfide bonds are formed between the side chains of cysteine by oxidation of two thiol groups (SH) to form a disulfide bond (S-S), also sometimes called a disulfide bridge. Quaternary Structure Quaternary structure is used to describe ...

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by biobitch
Tue May 25, 2010 4:37 am
 
Forum: Molecular Biology
Topic: Protein bonding(antigens)
Replies: 8
Views: 7939
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