4.2.2.11: guluronate-specific alginate lyase

This is an abbreviated version!
For detailed information about guluronate-specific alginate lyase, go to the full flat file.

Reaction

Synonyms

A1m, A9mC, A9mL, A9mT, Alg17C, Alg2A, Alg7D, AlgB, alginase II, alginate (poly-alpha-L-guluronate) lyase, alginate lyase, AlgL, AlgL5, AlgMytC, alkaliphilic alginate lyase, ALY, Aly-SJ02, Aly1, Aly5, AlyA, AlyA1PL7, AlyA5, AlyD, AlyDW11, AlyE, AlyQ, AlyV5, AXE80_11190, endo-type alginate lyase, guluronate lyase, KJ-2 alginate lyase, L-guluronan lyase, L-guluronate lyase, lyase, polyguluronate, Oal17A, oligoalginate lyase, poly(1,4-alpha-L-guluronide)lyase, poly(alpha-L-guluronate) lyase, poly-alpha-L-guluronate lyase, polyguluronate-specific alginate lyase, polyMG-specific alginate lyase, V12B01_09446, V12B01_24274, WP_053404615, xadAly7B

ECTree

     4 Lyases

         4.2 Carbon-oxygen lyases

             4.2.2 Acting on polysaccharides

                4.2.2.11 guluronate-specific alginate lyase

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Results	in table
6	Activating Compound
47	AA Sequence
15	Application
1	CAS Registry Number
28	Cloned(Commentary)
8	Crystallization (Commentary)
1	Expression
18	General Information
4	General Stability
131	Inhibitors
28	kcat/KM [mM/s]
48	KM Value [mM]
25	Localization
124	Metals/Ions
57	Molecular Weight [Da]
32	Natural Substrates/ Products (Substrates)
118	Organism
3	Pathway
5	PDB ID
55	pH Optimum
17	pH Range
23	pH Stability
24	pI Value
7	Posttranslational Modification
36	Protein Variants
28	Purification (Commentary)
7	Reaction
3	Reaction Type
101	Reference
3	Renatured (Commentary)
5	Source Tissue
38	Specific Activity [micromol/min/mg]
3	Storage Stability
261	Substrates and Products (Substrate)
71	Subunits
77	Synonyms
1	Systematic Name
48	Temperature Optimum [°C]
14	Temperature Range [°C]
36	Temperature Stability [°C]
31	Turnover Number [1/s]

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

6M urea collapses the circular dicroic spectral bands of the native enzyme caused by aromatic amino acids side chains and causes dissapearance of the enzyme activity, removal of the denaturant by dialysis restored the native-like spectrum and the activity, but some parts of the enzyme conformation are defective in the renaturation conditions

Corynebacterium sp.

-

648527

enzyme is not thermotolerant, but can refold to its active form following an almost complete denaturation at approximately 60°C

Shewanella sp. YH1

-

748129

solubilization of enzyme from inclusion bodies by 8 M urea in Tris-HCl, pH 8.0

Saccharophagus sp. Myt-1

L8B3Z6

730184