4.4.1.13: cysteine-S-conjugate beta-lyase

This is an abbreviated version!
For detailed information about cysteine-S-conjugate beta-lyase, go to the full flat file.

Reaction

Synonyms

AAR, beta-cystathionase, beta-lyase, C-DES, C-S lyase, CBL, CBL/ALR, CBS, CCBL2, Ctl1, Ctl2, cystathionine beta-lyase, cystathionine beta/gamma-lyase, cystathionine lyase, cysteine conjugate beta-lyase, cysteine conjugate. beta.-lyase, cysteine lyase, cysteine S-conjugate beta-lyase, cysteine-S-conjugate beta-lyase, cystine C-S lyase, cystine lyase, EC 4.4.1.6, EC 4.4.1.8, EcCBL, glutamine transaminase K, glutamine transaminase K/cysteine conjugate beta-lyase, GTK, Irc7p, KAT, KAT III, KYAT3, kynurenine aminotransferase, kynurenine-oxoglutarate transaminase 3, L-cystine C-S lyase, LACBS_00576, lyase, cystathionine beta-, lyase, cysteine conjugate.beta., MalY, MetC, More, Mp CBL, ORF5, osteotoxin, patB, PatB protein, Str3p, TmCBL, TTHA1620, wMelCBL

ECTree

     4 Lyases

         4.4 Carbon-sulfur lyases

             4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)

                4.4.1.13 cysteine-S-conjugate beta-lyase

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Results	in table
8	Activating Compound
11220	AA Sequence
11	Application
2	CAS Registry Number
36	Cloned(Commentary)
71	Cofactor
6	Crystallization (Commentary)
99	Disease/ Diagnostics
4	Expression
44	General Information
11	General Stability
30	IC50 Value
148	Inhibitors
41	kcat/KM [mM/s]
11	Ki Value [mM]
137	KM Value [mM]
40	Localization
2	Metals/Ions
56	Molecular Weight [Da]
48	Natural Substrates/ Products (Substrates)
167	Organism
20	Pathway
32	PDB ID
43	pH Optimum
13	pH Range
5	pH Stability
2	pI Value
2	Posttranslational Modification
42	Protein Variants
59	Purification (Commentary)
11	Reaction
19	Reaction Type
161	Reference
1	Renatured (Commentary)
90	Source Tissue
37	Specific Activity [micromol/min/mg]
18	Storage Stability
421	Substrates and Products (Substrate)
47	Subunits
127	Synonyms
1	Systematic Name
25	Temperature Optimum [°C]
2	Temperature Range [°C]
20	Temperature Stability [°C]
41	Turnover Number [1/s]

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

urea-induced unfolding, unfolding proceeds in at least three stages.The first transition, occurring between 0 and 1 M urea, gives rise to a partially active dimeric species that binds pyridoxal 5'-phosphate. The second equilibrium transition involving dimer dissociation, release of pyridoxal 5'-phosphate and loss of lyase activity leads to the formation of a monomeric equilibrium intermediate. It is a partially unfolded molecule that retains most of the native-state secondary structure, binds significant amounts of 8-anilino-1-naphthalenesulfonic acid (a probe for exposed hydro-phobic surfaces) and tends to self-associate. The self-associated aggregates predominate at urea concentrations of 2–4 M for holoMalY. The third step represents the complete unfolding of the enzyme. Both holo-and apo-MalY can be successfully refolded into the active enzyme with an 85% yield. Large misfolded soluble aggregates cannot be refolded and can be responsible for the incomplete reactivation

Escherichia coli

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663964