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Literature summary for 1.1.1.376 extracted from

  • Yoshiwara, K.; Watanabe, S.; Watanabe, Y.
    Crystal structure of bacterial L-arabinose 1-dehydrogenase in complex with L-arabinose and NADP (2020), Biochem. Biophys. Res. Commun., 530, 203-208 .
    View publication on PubMed
Search for more literature for 1.1.1.376

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3) Azospirillum brasilense
gene with a N-terminal (His)6-tag is expressed in Escherichia coli BL21(DE3) cells Azospirillum brasilense

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure in complex with L-arabinose and NADP+ Azospirillum brasilense
sitting-drop vapor diffusion method at 20°C Azospirillum brasilense

Protein Variants

Protein Variants Comment Organism
H119N kcat/KM for L-arabinose is 8088fold lower than the wild-type value Azospirillum brasilense
H119N mutant emzyme is significantly active, Km value is markedly higher (4450fold) than that of wild-type Azospirillum brasilense
H119N/N173H mutant enzyme is completely inactive Azospirillum brasilense
H119N/N173Y mutant enzyme is completely inactive Azospirillum brasilense
N173A kcat/KM for L-arabinose is 6111fold lower than the wild-type value Azospirillum brasilense
N173A strong decrease kcat/Km Azospirillum brasilense
N173D mutant enzyme is completely inactive Azospirillum brasilense
N173G kcat/KM for L-arabinose is 3427fold lower than the wild-type value Azospirillum brasilense
N173G strong decrease kcat/Km Azospirillum brasilense
N173H mutant enzyme is completely inactive Azospirillum brasilense
N173Q kcat/KM for L-arabinose is 9735fold lower than the wild-type value Azospirillum brasilense
N173Q strong decrease kcat/Km Azospirillum brasilense
N173S kcat/KM for L-arabinose is 7051fold lower than the wild-type value Azospirillum brasilense
N173S strong decrease kcat/Km Azospirillum brasilense
N173V kcat/KM for L-arabinose is 1874fold lower than the wild-type value Azospirillum brasilense
N173V strong decrease kcat/Km Azospirillum brasilense
N173Y mutant enzyme is completely inactive Azospirillum brasilense
S37D 7.3fold increase in Km-value for NADP+ and 6.5fold decrease in KM-value for NAD+ Azospirillum brasilense
S37D/R38A mutant enzyme shows a complete reversal of coenzyme specificity. The kcat/Km value for NADP+ decreases further by 20fold from that of the S37D mutant, and the ratio of NADP+ to NAD+ is about 0.07 Azospirillum brasilense
W152A kcat/KM for L-arabinose is 106fold lower than the wild-type value Azospirillum brasilense
W152A the kcat/Km value by 2 orders of magnitude from wild-type enzyme Azospirillum brasilense
W152F kcat/KM for L-arabinose is 28.4fold lower than the wild-type value Azospirillum brasilense
W152F mutant shows an 14fold higher Km value than the W152Y mutant Azospirillum brasilense
W152H kcat/KM for L-arabinose is 2.8fold lower than the wild-type value Azospirillum brasilense
W152H kcat/Km value is similar to that of wild-type Azospirillum brasilense
W152Y kcat/KM for L-arabinose is 1.7fold lower than the wild-type value Azospirillum brasilense
W152Y kcat/Km value is similar to that of wild-type Azospirillum brasilense
W152Y mutant shows an 14fold higher Km value than the W152Y mutant Azospirillum brasilense
W231A kcat/KM for L-arabinose is 33.2fold lower than the wild-type value Azospirillum brasilense
W231A the kcat/Km value by 2 orders of magnitude from wild-type enzyme Azospirillum brasilense

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.082
-
 NADP+ 30°C, pH 9.0, wild-type enzyme Azospirillum brasilense
0.082
-
 NADP+ pH 9.0, 30°C, wild-type enzyme Azospirillum brasilense
0.137
-
 NADP+ 30°C, pH 9.0, mutant enzyme R38A Azospirillum brasilense
0.137
-
 NADP+ pH 9.0, 30°C, mutant enzyme R38A Azospirillum brasilense
0.168
-
 L-arabinose 30°C, pH 9.0, wild-type enzyme Azospirillum brasilense
0.168
-
 L-arabinose pH 9.0, 30°C, wild-type enzyme Azospirillum brasilense
0.18
-
 NADP+ 30°C, pH 9.0, mutant enzyme S37D/R38A Azospirillum brasilense
0.18
-
 NADP+ pH 9.0, 30°C, mutant enzyme S37D/R38A Azospirillum brasilense
0.539
-
 NAD+ 30°C, pH 9.0, mutant enzyme S37D Azospirillum brasilense
0.539
-
 NAD+ pH 9.0, 30°C, mutant enzyme S37D Azospirillum brasilense
0.588
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W152Y Azospirillum brasilense
0.588
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W152Y Azospirillum brasilense
0.602
-
 NADP+ 30°C, pH 9.0, mutant enzyme S37D Azospirillum brasilense
0.602
-
 NADP+ pH 9.0, 30°C, mutant enzyme S37D Azospirillum brasilense
0.879
-
 NAD+ 30°C, pH 9.0, mutant enzyme S37D/R38A Azospirillum brasilense
0.879
-
 NAD+ pH 9.0, 30°C, mutant enzyme S37D/R38A Azospirillum brasilense
1.02
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W152H Azospirillum brasilense
1.02
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W152H Azospirillum brasilense
1.16
-
 NAD+ 30°C, pH 9.0, mutant enzyme R38A Azospirillum brasilense
1.16
-
 NAD+ pH 9.0, 30°C, mutant enzyme R38A Azospirillum brasilense
3.5
-
 NAD+ 30°C, pH 9.0, wild-type enzyme Azospirillum brasilense
3.5
-
 NAD+ pH 9.0, 30°C, wild-type enzyme enzyme Azospirillum brasilense
8.47
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W152F Azospirillum brasilense
8.47
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W152F Azospirillum brasilense
15.8
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173A Azospirillum brasilense
15.8
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173A Azospirillum brasilense
16
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173S Azospirillum brasilense
16
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173S Azospirillum brasilense
21.7
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W231A Azospirillum brasilense
21.7
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W231A Azospirillum brasilense
22.1
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173V Azospirillum brasilense
22.1
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173V Azospirillum brasilense
22.7
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173G Azospirillum brasilense
22.7
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173G Azospirillum brasilense
29
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173Q Azospirillum brasilense
29
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173Q Azospirillum brasilense
59.6
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W152A Azospirillum brasilense
59.6
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W152A Azospirillum brasilense
748
-
 L-arabinose 30°C, pH 9.0, mutant enzyme H119N Azospirillum brasilense
748
-
 L-arabinose pH 9.0, 30°C, mutant enzyme H119N Azospirillum brasilense

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arabinose + NAD+ Azospirillum brasilense
-
 L-arabinono-1,4-lactone + NADH + H+
-
 ?
L-arabinose + NAD+ Azospirillum brasilense ATCC 29145
-
 L-arabinono-1,4-lactone + NADH + H+
-
 ?
L-arabinose + NADP+ Azospirillum brasilense
-
 L-arabinono-1,4-lactone + NADPH + H+
-
 ?
L-arabinose + NADP+ Azospirillum brasilense ATCC 29145
-
 L-arabinono-1,4-lactone + NADPH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Azospirillum brasilense Q53TZ2
-
-
Azospirillum brasilense ATCC 29145 Q53TZ2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Azospirillum brasilense

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arabinose + NAD+
-
 Azospirillum brasilense L-arabinono-1,4-lactone + NADH + H+
-
 ?
L-arabinose + NAD+ preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38 Azospirillum brasilense L-arabinono-1,4-lactone + NADH + H+
-
 ?
L-arabinose + NAD+
-
 Azospirillum brasilense ATCC 29145 L-arabinono-1,4-lactone + NADH + H+
-
 ?
L-arabinose + NAD+ preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38 Azospirillum brasilense ATCC 29145 L-arabinono-1,4-lactone + NADH + H+
-
 ?
L-arabinose + NADP+
-
 Azospirillum brasilense L-arabinono-1,4-lactone + NADPH + H+
-
 ?
L-arabinose + NADP+ preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38 Azospirillum brasilense L-arabinono-1,4-lactone + NADPH + H+
-
 ?
L-arabinose + NADP+
-
 Azospirillum brasilense ATCC 29145 L-arabinono-1,4-lactone + NADPH + H+
-
 ?
L-arabinose + NADP+ preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38 Azospirillum brasilense ATCC 29145 L-arabinono-1,4-lactone + NADPH + H+
-
 ?

Synonyms

Synonyms Comment Organism
AraDH
-
 Azospirillum brasilense
L-arabinose 1-dehydrogenase
-
 Azospirillum brasilense

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.417
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173S Azospirillum brasilense
0.42
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173S Azospirillum brasilense
0.47
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173A Azospirillum brasilense
0.47
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173A Azospirillum brasilense
0.54
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173Q Azospirillum brasilense
0.54
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173Q Azospirillum brasilense
0.98
-
 NADP+ 30°C, pH 9.0, mutant enzyme S37D/R38A Azospirillum brasilense
0.98
-
 NADP+ pH 9.0, 30°C, mutant enzyme S37D/R38A Azospirillum brasilense
1.175
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173G Azospirillum brasilense
1.18
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173G Azospirillum brasilense
2.17
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173V Azospirillum brasilense
2.2
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173V Azospirillum brasilense
6.4
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W152Y Azospirillum brasilense
6.43
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W152Y Azospirillum brasilense
17
-
 L-arabinose 30°C, pH 9.0, mutant enzyme H119N Azospirillum brasilense
17
-
 L-arabinose pH 9.0, 30°C, mutant enzyme H119N Azospirillum brasilense
30.5
-
 L-arabinose pH 9.0, 30°C, wild-type enzyme Azospirillum brasilense
30.5
-
 L-arabinose 30°C, pH 9.0, wild-type enzyme Azospirillum brasilense
48.7
-
 NAD+ 30°C, pH 9.0, wild-type enzyme Azospirillum brasilense
48.7
-
 NAD+ pH 9.0, 30°C, wild-type enzyme enzyme Azospirillum brasilense
54.3
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W152F Azospirillum brasilense
54.3
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W152F Azospirillum brasilense
66.5
-
 NADP+ 30°C, pH 9.0, mutant enzyme S37D Azospirillum brasilense
66.5
-
 NADP+ pH 9.0, 30°C, mutant enzyme S37D Azospirillum brasilense
66.7
-
 NADP+ pH 9.0, 30°C, wild-type enzyme Azospirillum brasilense
66.7
-
 NADP+ 30°C, pH 9.0, wild-type enzyme Azospirillum brasilense
67.33
-
 NAD+ 30°C, pH 9.0, mutant enzyme S37D/R38A Azospirillum brasilense
67.33
-
 NAD+ pH 9.0, 30°C, mutant enzyme S37D/R38A Azospirillum brasilense
68
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W152H Azospirillum brasilense
68
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W152H Azospirillum brasilense
72.2
-
 NAD+ 30°C, pH 9.0, mutant enzyme S37D Azospirillum brasilense
72.2
-
 NAD+ pH 9.0, 30°C, mutant enzyme S37D Azospirillum brasilense
83
-
 NAD+ 30°C, pH 9.0, mutant enzyme R38A Azospirillum brasilense
83
-
 NAD+ pH 9.0, 30°C, mutant enzyme R38A Azospirillum brasilense
102.8
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W152A Azospirillum brasilense
102.8
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W152A Azospirillum brasilense
119.8
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W231A Azospirillum brasilense
119.8
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W231A Azospirillum brasilense
175
-
 NADP+ 30°C, pH 9.0, mutant enzyme R38A Azospirillum brasilense
175
-
 NADP+ pH 9.0, 30°C, mutant enzyme R38A Azospirillum brasilense

Cofactor

Cofactor Comment Organism Structure
NAD+ preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38 Azospirillum brasilense
NAD+ preference of NADP+ over NAD+, wild-type enzyme. Mutant enzyme S37D/R38A shows a complete reversal of coenzyme specificity Azospirillum brasilense
NADP+ preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38 Azospirillum brasilense
NADP+ preference of NADP+ over NAD+, wild-type enzyme. Mutant enzyme S37D/R38A shows a complete reversal of coenzyme specificity Azospirillum brasilense

General Information

General Information Comment Organism
metabolism the enzyme is responsible for the first step of the non-phosphorylative L-arabinose pathway from bacteria Azospirillum brasilense

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.019
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173Q Azospirillum brasilense
0.019
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173Q Azospirillum brasilense
0.023
-
 L-arabinose 30°C, pH 9.0, mutant enzyme H119N Azospirillum brasilense
0.023
-
 L-arabinose pH 9.0, 30°C, mutant enzyme H119N Azospirillum brasilense
0.026
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173S Azospirillum brasilense
0.026
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173S Azospirillum brasilense
0.03
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173A Azospirillum brasilense
0.03
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173A Azospirillum brasilense
0.0535
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173G Azospirillum brasilense
0.054
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173G Azospirillum brasilense
0.098
-
 L-arabinose 30°C, pH 9.0, mutant enzyme N173V Azospirillum brasilense
0.098
-
 L-arabinose pH 9.0, 30°C, mutant enzyme N173V Azospirillum brasilense
1.7
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W152A Azospirillum brasilense
1.7
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W152A Azospirillum brasilense
5.3
-
 NADP+ 30°C, pH 9.0, mutant enzyme S37D/R38A Azospirillum brasilense
5.47
-
 NADP+ pH 9.0, 30°C, mutant enzyme S37D/R38A Azospirillum brasilense
5.5
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W231A Azospirillum brasilense
5.52
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W231A Azospirillum brasilense
6.45
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W152F Azospirillum brasilense
6.45
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W152F Azospirillum brasilense
13.9
-
 NAD+ 30°C, pH 9.0, wild-type enzyme Azospirillum brasilense
13.9
-
 NAD+ pH 9.0, 30°C, wild-type enzyme enzyme Azospirillum brasilense
66.5
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W152H Azospirillum brasilense
66.5
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W152H Azospirillum brasilense
71.6
-
 NAD+ 30°C, pH 9.0, mutant enzyme R38A Azospirillum brasilense
71.8
-
 NAD+ pH 9.0, 30°C, mutant enzyme R38A Azospirillum brasilense
76.6
-
 NAD+ 30°C, pH 9.0, mutant enzyme S37D/R38A Azospirillum brasilense
77.5
-
 NAD+ pH 9.0, 30°C, mutant enzyme S37D/R38A Azospirillum brasilense
109.8
-
 L-arabinose 30°C, pH 9.0, mutant enzyme W152Y Azospirillum brasilense
109.8
-
 L-arabinose pH 9.0, 30°C, mutant enzyme W152Y Azospirillum brasilense
110.5
-
 NADP+ 30°C, pH 9.0, mutant enzyme S37D Azospirillum brasilense
110.5
-
 NADP+ pH 9.0, 30°C, mutant enzyme S37D Azospirillum brasilense
133.8
-
 NAD+ pH 9.0, 30°C, mutant enzyme S37D Azospirillum brasilense
140
-
 NAD+ 30°C, pH 9.0, mutant enzyme S37D Azospirillum brasilense
183
-
 L-arabinose 30°C, pH 9.0, wild-type enzyme Azospirillum brasilense
183.3
-
 L-arabinose pH 9.0, 30°C, wild-type enzyme Azospirillum brasilense
810
-
 NADP+ pH 9.0, 30°C, wild-type enzyme Azospirillum brasilense
813.4
-
 NADP+ 30°C, pH 9.0, wild-type enzyme Azospirillum brasilense
1275
-
 NADP+ pH 9.0, 30°C, mutant enzyme R38A Azospirillum brasilense
1277
-
 NADP+ 30°C, pH 9.0, mutant enzyme R38A Azospirillum brasilense